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Crystallization and preliminary X-ray crystallographic analysis of γ-carboxymucolactone decarboxylase from Sulfolobus solfataricusEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
γ-Carboxymucolactone decarboxylase (γ-CMD; EC 4.1.1.44) catalyzes the conversion of γ-carboxymucolactone to β-ketoadipate enol-lactone in the β-ketoadipate pathway, which is a key part of the degradation process of aromatic compounds in bacteria and in some eukaryotes such as fungi and yeast. γ-CMD from the thermophilic archaeon Sulfolobus solfataricus (Ss γ-CMD) is encoded by the pcaC gene and is composed of 139 amino-acid residues with a molecular mass of 15 945 Da. Ss γ-CMD was crystallized and X-ray data were collected to 2.40 Å resolution. The crystal belonged to space group P43212, with unit-cell param...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Lee, H.Y.Yang, J.K. Tags: γ -carboxymucolactone decarboxylase PcaC Sulfolobus solfataricus crystallization communications Source Type: journals

Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylaseEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
An archaeal-type phosphoenolpyruvate carboxylase (PepcA) from Clostridium perfringens has been expressed in Escherichia coli in a soluble form with an amino-terminal His tag. The recombinant protein is enzymatically active and two crystal forms have been obtained. Complete diffraction data extending to 3.13 Å resolution have been measured from a crystal soaked in KAu(CN)2, using radiation at a wavelength just above the Au LIII edge. The asymmetric unit contains two tetramers of PepcA. (Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Dharmarajan, L.Kraszewski, J.L.Mukhopadhyay, B.Dunten, P.W. Tags: phosphoenolpyruvate carboxylase Clostridium perfringens crystallization communications Source Type: journals

Purification, crystallization and preliminary X-ray analysis of β-glucosidase from Kluyveromyces marxianus NBRC1777Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The intracellular β-glucosidase from Kluyveromyces marxianus NBRC1777 (KmBglI) belongs to glycoside hydrolase family 3 and has a unique domain architecture. Selenomethionine-labelled KmBglI was purified and crystallized by the hanging-drop vapour-diffusion method using the purified enzyme at 30 mg ml−1, 0.04 M potassium dihydrogen phosphate pH 5.1, 16%(w/v) PEG 8000 and 20%(v/v) glycerol. The crystal belonged to space group C2, with unit-cell parameters a = 245.8, b = 148.7, c = 119.9 Å, β = 112.9°. Multiple-wavelength anomalous dispersion data were collected at 2.4 and 2.5 Å resolution. A tetramer was ass...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Yoshida, E.Hidaka, M.Fushinobu, S.Koyanagi, T.Minami, H.Tamaki, H.Kitaoka, M.Katayama, T.Kumagai, H. Tags: β -glucosidases Kluyveromyces marxianus NBRC1777 glycoside hydrolase family 3 crystallization communications Source Type: journals

Crystallization and initial X-ray diffraction study of the three PASTA domains of the Ser/Thr kinase Stk1 from the human pathogen Staphylococcus aureusEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
PASTA subunits (∼70 amino acids) are specific to bacterial serine/threonine kinases and to penicillin-binding proteins (PBPs) and are involved in the synthesis of peptidoglycan. The human pathogen Staphylococcus aureus contains a serine/threonine kinase, Stk1, which plays a major role in virulence. A recombinant His-tagged portion of the extracellular domain of Stk1 containing three PASTA subunits has been crystallized using zinc sulfate as a crystallizing agent. The crystals belonged to the tetragonal space group P4122, with unit-cell parameters a = 68.0, b = 68.0, c = 158.1 Å. Structure determination by the MAD met...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Paracuellos, P.Ballandras, A.Robert, X.Cozzone, A.J.Duclos, B.Gouet, P. Tags: Staphylococcus aureus Ser/Thr kinases PASTA subunits crystallization communications Source Type: journals

Purification, crystallization and preliminary X-ray diffraction experiments on the breakage-reunion domain of the DNA gyrase from Mycobacterium tuberculosisEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Mycobacterium tuberculosis DNA gyrase, a nanomachine that is involved in the regulation of DNA topology, is the only type II topoisomerase present in this organism and hence is the sole target for fluoroquinolone action. The breakage-reunion domain of the A subunit plays an essential role in DNA binding during the catalytic cycle. Two constructs of 53 and 57 kDa (termed GA53BK and GA57BK) corresponding to this domain have been overproduced, purified and crystallized. Diffraction data were collected from four crystal forms. The resolution limits ranged from 4.6 to 2.7 Å depending on the crystal form. The best diffract...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Piton, J.Matrat, S.Petrella, S.Jarlier, V.Aubry, A.Mayer, C. Tags: tuberculosis Mycobacterium tuberculosis type II topoisomerase DNA gyrase antibiotic resistance crystallization communications Source Type: journals

Crystallization and preliminary X-ray diffraction analysis of the complex of Kunitz-type tamarind trypsin inhibitor and porcine pancreatic trypsinEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The complex of Tamarindus indica Kunitz-type trypsin inhibitor and porcine trypsin has been crystallized by the sitting-drop vapour-diffusion method using ammonium acetate as precipitant and sodium acetate as buffer. The homogeneity of complex formation was checked by size-exclusion chromatography and further confirmed by reducing SDS–PAGE. The crystals diffracted to 2.0 Å resolution and belonged to the tetragonal space group P41, with unit-cell parameters a = b = 57.1, c = 120.1 Å. Preliminary X-ray diffraction analysis indicated the presence of one unit of inhibitor–trypsin complex per asymmetric unit, with...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Tomar, S.Patil, D.N.Datta, M.Tapas, S.PreetiChaudhary, A.Sharma, A.K.Tomar, S.Kumar, P. Tags: tamarind trypsin inhibitor porcine pancreatic trypsin Kunitz-type inhibitors crystallization communications Source Type: journals

Crystallization and preliminary crystallographic studies of dihydrofolate reductase-thymidylate synthase from Trypanosoma cruzi, the Chagas disease pathogenEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Trypanosoma cruzi dihydrofolate reductase-thymidylate synthase (TcDHFR-TS) was crystallized in complexes with the dihydrotriazine-based or quinazoline-based antifolates C-448, cycloguanil (CYC) and Q-8 in order to gain insight into the interactions of this DHFR enzyme with classical and novel inhibitors. The TcDHFR-TS–C-448–NDP–dUMP crystal belonged to space group C2221 with two molecules per asymmetric unit and diffracted to 2.37 Å resolution. The TcDHFR-TS–CYC, TcDHFR-TS–CYC–NDP and TcDHFR-TS–Q-8–NDP crystals belonged to space group P21 with four molecules per asymmetric unit and diffracted to 2.1, 2.6...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Chitnumsub, P.Yuvaniyama, J.Chahomchuen, T.Vilaivan, T.Yuthavong, Y. Tags: dihydrofolate reductase-thymidylate synthase Trypanosoma cruzi Chagas disease antifolates crystallization communications Source Type: journals

Crystallization and preliminary crystallographic analysis of gallate dioxygenase DesB from Sphingobium sp. SYK-6Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Gallate dioxygenase (DesB) from Sphingobium sp. SYK-6, which belongs to the type II extradiol dioxygenase family, was purified and crystallized using the hanging-drop vapour-diffusion method. Two crystal forms were obtained. The form I crystal belonged to space group C2, with unit-cell parameters a = 136.2, b = 53.6, c = 55.1 Å, β = 112.8°, and diffracted to 1.6 Å resolution. The form II crystal belonged to space group P21, with unit-cell parameters a = 56.2, b = 64.7, c = 116.1 Å, β = 95.1°, and diffracted to 1.9 Å resolution. A molecular-replacement calculation using LigAB as a search model yielded a sat...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Sugimoto, K.Yamamoto, Y.Antoni, S.Senda, M.Kasai, D.Masai, E.Fukuda, M.Senda, T. Tags: extradiol dioxygenases gallate dioxygenase crystallization communications Source Type: journals

Purification, crystallization and preliminary X-ray diffraction analysis of disease-related mutants of p97Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The human type II AAA+ protein p97 participates in various cellular activities, presumably through its involvement in the ubiquitin–proteasome degradation pathway. Mutations in p97 have been implicated in patients with inclusion-body myopathy associated with Paget's disease of the bone and frontotemporal dementia (IBMPFD). In this work, three mutant p97 N-D1 fragments, R86A, R95G and R155H, were crystallized in the presence of ATPγS with PEG 3350 as a main precipitant, yielding two different crystal forms. The R155H mutant crystal belonged to space group R3, with unit-cell parameters in the hexagonal setting of a = b = ...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Tang, W.-K.Li, D.Esser, L.Xia, D. Tags: p97 AAA proteins disease-related mutants crystallization communications Source Type: journals

Crystallization and preliminary X-ray diffraction analysis of the fructofuranosidase from Schwanniomyces occidentalisEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Schwanniomyces occidentalis invertase is an extracellular enzyme that releases β-fructose from the nonreducing termini of various β-d-fructofuranoside substrates. Its ability to produce 6-kestose by transglycosylation makes this enzyme an interesting research target for applications in industrial biotechnology. The enzyme has been expressed in Saccharomyces cerevisiae. Recombinant and wild-type forms, which showed different glycosylation patterns, were crystallized by vapour-diffusion methods. Although crystallization trials were conducted on both forms of the protein, crystals suitable for X-ray crystallographic analyse...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Polo, A.Álvaro-Benito, M.Fernández-Lobato, M.Sanz-Aparicio, J. Tags: yeast invertases fructofuranosidases glycoside hydrolase family 32 crystallization communications Source Type: journals

Crystallization and preliminary X-ray crystallographic characterization of a public CMV-specific TCR in complex with its cognate antigenEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The T-cell response to human cytomegalovirus is characterized by a dramatic reduction of clonal diversity in patients undergoing chronic inflammation or immunodepression. In order to check whether all the selected high-avidity T-cell clones recognize the immunodominant pp65 peptide antigen pp65495–503 (NLVPMVATV) presented by the major histocompatibility complex (MHC) molecule HLA-A2 in a similar manner, several public high-affinity T-cell receptors (TCRs) specific for the pp65495–503–HLA-A2 complex have been investigated. Expression, purification and crystallization were performed and preliminary crystallographic da...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Reiser, J.-B.Legoux, F.Machillot, P.Debeaupuis, E.Le Moullac-Vaydie, B.Chouquet, A.Saulquin, X.Bonneville, M.Housset, D. Tags: T-cell receptors human cytomegalovirus HLA-A2 public response affinity selection crystallization communications Source Type: journals

Purification, crystallization and preliminary X-ray analysis of bifunctional isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coliEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Escherichia coli isocitrate dehydrogenase (ICDH) can be phosphorylated and dephosphorylated by a single bifunctional protein, isocitrate dehydrogenase kinase/phosphatase (AceK), which is encoded by the aceK gene. In order to investigate the regulatory mechanism of (de)phosphorylation of ICDH by AceK, AceK was successfully cocrystallized in complex with its intact protein substrate, ICDH, in the presence of ATP. The complex crystal was obtained by the hanging-drop vapour-diffusion technique using PEG 300 as a precipitant and magnesium sulfate as an additive. SDS–PAGE analysis of dissolved crystals showed that the crystal...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Zheng, J.Ji, A.X.Jia, Z. Tags: isocitrate dehydrogenases Ser/Thr protein kinases protein phosphatases citric acid cycle glyoxylate bypass AceK – protein complexes crystallization communications Source Type: journals

Crystallization of the head and galectin-like domains of porcine adenovirus isolate NADC-1 fibreEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The porcine adenovirus NADC-1 isolate, a strain of porcine adenovirus type 4, has a fibre with an atypical architecture. In addition to a classical virus-attachment region, shaft and head domains, it contains an additional galectin-like domain C-terminal to the head domain and connected to the head domain by a long RGD-containing loop. The galectin-like domain contains two putative carbohydrate-recognition domains. The head and galectin-like domains have been independently crystallized. Diffraction data have been obtained to 3.2 Å resolution from crystals of the head domain and to 1.9 Å resolution from galectin-like ...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Guardado-Calvo, P.Llamas-Saiz, A.L.Fox, G.C.Glasgow, J.N.van Raaij, M.J. Tags: porcine adenovirus NADC-1 isolate adenoviruses head domain galectin-like domain crystallization communications Source Type: journals

Expression, purification, crystallization and preliminary X-ray analysis of conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708 is a member of the NADPH-dependent aldo-keto reductase (AKR) superfamily and catalyzes the stereospecific reduction of ketopantoyl lactone to d-pantoyl lactone. A diffraction-quality crystal of recombinant CPR-C2 was obtained by the sitting-drop vapour-diffusion method using PEG 3350 as the precipitant. The crystal diffracted X-rays to 1.7 Å resolution on beamline NW12A of the Photon Factory-Advanced Ring (Tsukuba, Japan). The crystal belonged to space group P212121, with unit-cell parameters a = 55.02, b = 68.30, c = 68.93 Å. The Matthe...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Yamamura, A.Maruoka, S.Ohtsuka, J.Miyakawa, T.Nagata, K.Kataoka, M.Kitamura, N.Shimizu, S.Tanokura, M. Tags: conjugated polyketone reductase C Candida parapsilosis NAD(P)H-dependent oxidoreductases crystallization communications Source Type: journals

Overexpression, crystallization and preliminary X-ray crystallographic analysis of d-ribose-5-phosphate isomerase from Clostridium thermocellumEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Rare sugars are used for many industrial and medical purposes and are produced by the interconversion between aldoses and ketoses catalyzed by sugar and sugar-phosphate isomerases. Recently, Clostridium thermocellum d-ribose-5-phosphate isomerase (CTRPI), an aldose–ketose isomerase, was cloned in order to synthesize d-allose and its substrate specificity was further characterized for industrial usage. CTRPI has a novel substrate specificity that differs from those of other isomerases, which have broad substrate specificities. CTRPI prefers aldose substrates such as l-talose, d-ribose and d-allose. CTRPI was purified and ...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Jung, J.Yeom, S.-J.Kim, J.Kim, J.-K.Natarajan, S.Ahn, Y.-J.Lim, S.B.Oh, D.-K.Kang, L.-W. Tags: d-ribose phosphate isomerases CTRPI isomerization crystallization communications Source Type: journals

Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
In this report, a series of mutations at this crystal contact designed to both reduce side-chain entropy and replace the solvent-mediated interface with direct side-chain contacts are reported. The results suggest that improved crystal growth is achieved upon the introduction of direct crystal contacts, while little improvement is observed with side-chain entropy-reducing mutations alone. (Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Meher, A.K.Blaber, S.I.Lee, J.Honjo, E.Kuroki, R.Blaber, M. Tags: protein crystallization side-chain entropy neutron diffraction protein engineering crystal growth crystallization communications Source Type: journals

Recombinant production, crystallization and preliminary X-ray analysis of PCNA from the psychrophilic archaeon Methanococcoides burtonii DSM 6242Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Proliferating cell nuclear antigen (PCNA) is a DNA-clamping protein that is responsible for increasing the processivity of the replicative polymerases during DNA replication and repair. The PCNA from the eurypsychrophilic archaeon Methanococcoides burtonii DSM 6242 (MbPCNA) has been targeted for protein structural studies. A recombinant expression system has been created that overproduces MbPCNA with an N-terminal hexahistidine affinity tag in Escherichia coli. As a result, recombinant MbPCNA with a molecular mass of 28.3 kDa has been purified to at least 95% homogeneity and crystallized by vapor-diffusion equilibration....
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Byrne-Steele, M.L.Hughes, R.C.Ng, J.D. Tags: PCNA DNA replication archaea psychrophiles cold adaptation crystallization communications Source Type: journals

Crystallization and preliminary X-ray analysis of the stress-response PPM phosphatase RsbX from Bacillus subtilisEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
RsbX from Bacillus subtilis is a manganese-dependent PPM phosphatase and negatively regulates the signal transduction of the general stress response by the dephosphorylation of RsbS and RsbR, which are activators of the alternative RNA polymerase σ factor SigB. In order to elucidate the structural–functional relationship of its Ser/Thr protein-phosphorylation mechanism, an X-ray crystallographic diffraction study of RsbX was performed. Recombinant RsbX was expressed in Escherichia coli, purified and crystallized. Crystals were obtained using the sitting-drop vapour-diffusion method and X-ray diffraction data were collec...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Suganuma, M.Teh, A.H.Makino, M.Shimizu, N.Kaneko, T.Hirata, K.Yamamoto, M.Kumasaka, T. Tags: PPM phosphatases RsbX general stress response Bacillus subtilis crystallization communications Source Type: journals

Crystallization and preliminary crystallographic analysis of the global nitrogen regulator AmtR from Corynebacterium glutamicumEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
AmtR, a member of the TetR family of transcription regulators, is a global regulator of nitrogen control in Corynebacterium glutamicum. Unlike other TetR-family members, which are regulated by small-molecule effectors, AmtR is regulated by a protein called GlnK. It has been shown that a GlnK trimer has to become adenylylated prior to formation of a complex with AmtR. The physiological function of AmtR has been very well studied, but structural characterization of the mechanistic aspects of AmtR-regulated transcription has yet to be accomplished. AmtR has successfully been crystallized in space group P21212, with six molec...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Hasselt, K.Sevvana, M.Burkovski, A.Muller, Y.A. Tags: nitrogen control bacterial transcription regulation SeMet phasing TetR family of repressors crystallization communications Source Type: journals

Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureusEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Free methionine-(R)-sulfoxide reductase (fRMsr) catalyzes the reduction of the free form of methionine-(R)-sulfoxide back to free methionine. The fRMsr protein from Staphylococcus aureus was overexpressed in Escherichia coli, purified and crystallized at 295 K using ammonium sulfate as a precipitant. Diffraction data were collected to 1.7 Å resolution from a native crystal using synchrotron radiation. The crystal belonged to the hexagonal space group P6122, with unit-cell parameters a = b = 89.84, c = 88.75 Å, α = β = 90, γ = 120°. Assuming the presence of one molecule in the asymmetric unit, the calculated Mat...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Bong, S.M.Moon, J.H.Kim, H.Y.Kim, H.S.Chi, Y.M.Kim, A.Y. Tags: methionine sulfoxide free methionine free methionine-(R)-sulfoxide reductase crystallization communications Source Type: journals

Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania majorEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Nucleoside diphosphate kinases (NDKs; EC 2.7.4.6) play an essential role in the synthesis of nucleotides from intermediates in the salvage pathway in all parasitic trypanosomatids and their structural studies will be instrumental in shedding light on the biochemical machinery involved in the parasite life cycle and host–parasite interactions. In this work, NDKb from Leishmania major was overexpressed in Escherichia coli, purified to homogeneity and crystallized using the sitting-drop vapour-diffusion method. The NDK crystal diffracted to 2.2 Å resolution and belonged to the trigonal crystal system, with unit-cell par...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Tonoli, C.C.C.Vieira, P.S.Ward, R.J.Arni, R.K.de Oliveira, A.H.C.Murakami, M.T. Tags: Leishmania major salvage pathway nucleoside diphosphate kinase b crystallization communications Source Type: journals

Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of an atypical two-cysteine peroxiredoxin (SAOUHSC_01822) from Staphylococcus aureus NCTC 8325Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
An atypical two-cysteine peroxidase, SAOUHSC_01822, from the virulent Staphylococcus aureus strain NCTC 8325 plays a major role in the reponse of the bacterium to oxidative stress. The protein was cloned, expressed, purified to homogeneity and crystallized. The protein was crystallized from 2 M ammonium sulfate, 0.1 M Na HEPES pH 7, 2%(v/v) PEG 400. A complete diffraction data set was collected to 2.3 Å resolution using a Rigaku MicroMax HF007 Cu Kα X-ray generator and a Rigaku R-AXIS IV++ detector. The crystals belonged to space group P21, with unit-cell parameters a = 43.50, b = 149.35, c = 73.73 Å, β = 1...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Bhattacharyya, S.Dutta, D.Ghosh, A.K.Das, A.K. Tags: peroxiredoxins Staphylococcus aureus SAOUHSC_01822 crystallization communications Source Type: journals

A preliminary X-ray study of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomalleiEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
In this study, GmhA has been cloned, expressed, purified and crystallized. Synchrotron X-ray data were also collected to 1.9 Å resolution. The crystal belonged to the primitive orthorhombic space group P212121, with unit-cell parameters a = 61.3, b = 84.2, c = 142.3 Å. A full structural determination is under way in order to provide insights into the structure–function relationships of this protein. (Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Kim, M.-S.Shin, D.H. Tags: sedoheptulose-7-phosphate isomerase Burkholderia pseudomallei crystallization communications Source Type: journals

Crystal optimization and preliminary diffraction data analysis of the Smad1 MH1 domain bound to a palindromic SBE DNA elementEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The bone morphogenetic protein (BMP) signalling pathway regulates diverse processes such as cell differentiation, anterior/posterior axis specification, cell growth and the formation of extra-embryonic tissues. The transcription factor Smad1 relays the BMP signal from the cytoplasm to the nucleus, where it binds short DNA-sequence motifs and regulates gene expression. However, how Smad1 selectively targets particular genomic regions is poorly understood. In order to understand the physical basis of the specific interaction of Smad1 with DNA and to contrast it with the highly homologous but functionally distinct Smad3 prote...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Baburajendran, N.Palasingam, P.Ng, C.K.L.Jauch, R.Kolatkar, P.R. Tags: Smad1 MH1 domain Smad-binding element crystallization communications Source Type: journals

X-ray structure and biophysical properties of rabbit fibroblast growth factor 1Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The rabbit is an important and de facto animal model in the study of ischemic disease and angiogenic therapy. Additionally, fibroblast growth factor 1 (FGF-1) is emerging as one of the most important growth factors for novel pro-angiogenic and pro-arteriogenic therapy. However, despite its significance, the fundamental biophysical properties of rabbit FGF-1, including its X-ray structure, have never been reported. Here, the cloning, crystallization, X-ray structure and determination of the biophysical properties of rabbit FGF-1 are described. The X-ray structure shows that the amino-acid differences between human and rabbi...
Source: Acta Crystallographica Section F - October 30, 2009 Category: Biochemistry Authors: Lee, J.Blaber, S.I.Irsigler, A.Aspinwall, E.Blaber, M. Tags: fibroblast growth factor angiogenesis FGF-1 rabbit ischemia structural communications Source Type: journals

The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulationEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Proteins with the DUF2063 domain constitute a new Pfam family, PF09836. The crystal structure of a member of this family, NGO1945 from Neisseria gonorrhoeae, has been determined and reveals that the N-terminal DUF2063 domain is likely to be a DNA-binding domain. In conjunction with the rest of the protein, NGO1945 is likely to be involved in transcriptional regulation, which is consistent with genomic neighborhood analysis. Of the 216 currently known proteins that contain a DUF2063 domain, the most significant sequence homologs of NGO1945 (∼40–99% sequence identity) are from various Neisseria and Haemophilus species. A...
Source: Acta Crystallographica Section F - October 28, 2009 Category: Biochemistry Authors: Das, D.Grishin, N.V.Kumar, A.Carlton, D.Bakolitsa, C.Miller, M.D.Abdubek, P.Astakhova, T.Axelrod, H.L.Burra, P.Chen, C.Chiu, H.-J.Chiu, M.Clayton, T.Deller, M.C.Duan, L.Ellrott, K.Ernst, D.Farr, C.L.Feuerhelm, J.Grzechnik, A.Grzechnik, S.K.Grant, J.C.Han, Tags: NGO1945 PF09836 DUF2063 putative DNA-binding proteins putative transcription regulators structural genomics structural communications Source Type: journals

Conformational changes associated with the binding of zinc acetate at the putative active site of XcTcmJ, a cupin from Xanthomonas campestris pv. campestrisEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
In the plant pathogen Xanthomonas campestris pv. campestris, the product of the tcmJ gene, XcTcmJ, encodes a protein belonging to the RmlC family of cupins. XcTcmJ was crystallized in a monoclinic space group (C2) in the presence of zinc acetate and the structure was determined to 1.6 Å resolution. Previously, the apo structure has been reported in the absence of any bound metal ion [Chin et al. (2006), Proteins, 65, 1046–1050]. The most significant difference between the apo structure and the structure of XcTcmJ described here is a reorganization of the binding site for zinc acetate, which was most likely acquired fr...
Source: Acta Crystallographica Section F - October 27, 2009 Category: Biochemistry Authors: Axelrod, H.L.Kozbial, P.McMullan, D.Krishna, S.S.Miller, M.D.Abdubek, P.Acosta, C.Astakhova, T.Carlton, D.Caruthers, J.Chiu, H.-J.Clayton, T.Deller, M.C.Duan, L.Elias, Y.Feuerhelm, J.Grzechnik, S.K.Grant, J.C.Han, G.W.Jaroszewski, L.Jin, K.K.Klock, H.E.Kn Tags: zinc-binding sites conformational changes metalloproteins ligand binding structural genomics structural communications Source Type: journals

The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-foldEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
KPN03535 (gi|152972051) is a putative lipoprotein of unknown function that is secreted by Klebsiella pneumoniae MGH 78578. The crystal structure reveals that despite a lack of any detectable sequence similarity to known structures, it is a novel variant of the OB-fold and structurally similar to the bacterial Cpx-pathway protein NlpE, single-stranded DNA-binding (SSB) proteins and toxins. K. pneumoniae MGH 78578 forms part of the normal human skin, mouth and gut flora and is an opportunistic pathogen that is linked to about 8% of all hospital-acquired infections in the USA. This structure provides the foundation for furthe...
Source: Acta Crystallographica Section F - October 27, 2009 Category: Biochemistry Authors: Das, D.Kozbial, P.Han, G.W.Carlton, D.Jaroszewski, L.Abdubek, P.Astakhova, T.Axelrod, H.L.Bakolitsa, C.Chen, C.Chiu, H.-J.Chiu, M.Clayton, T.Deller, M.C.Duan, L.Ellrott, K.Elsliger, M.-A.Ernst, D.Farr, C.L.Feuerhelm, J.Grzechnik, A.Grant, J.C.Jin, K.K.Joh Tags: lipoproteins OB-fold NipE-like protein single-stranded DNA-binding proteins toxins BOF human gut pathogens structural genomics structural communications Source Type: journals

Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolutionEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5 Å resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks some key structural features that are important for interaction with ATP. A conserved surface was identified, supporting its role in the formation of protein complexes. (Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - October 27, 2009 Category: Biochemistry Authors: Xu, Q.McMullan, D.Jaroszewski, L.Krishna, S.S.Elsliger, M.-A.Yeh, A.P.Abdubek, P.Astakhova, T.Axelrod, H.L.Carlton, D.Chiu, H.-J.Clayton, T.Duan, L.Feuerhelm, J.Grant, J.C.Han, G.W.Jin, K.K.Klock, H.E.Knuth, M.W.Miller, M.D.Morse, A.T.Nigoghossian, E.Okac Tags: YgjD YeaZ TM0874 essential genes protein complexes structural communications Source Type: journals

The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolismEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The crystal structure of PA1994 from Pseudomonas aeruginosa, a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15-stranded β-sheet wrapped around a single α-helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid-binding and sugar-binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome-context analysis lends further support to the involve...
Source: Acta Crystallographica Section F - October 27, 2009 Category: Biochemistry Authors: Bakolitsa, C.Kumar, A.McMullan, D.Krishna, S.S.Miller, M.D.Carlton, D.Najmanovich, R.Abdubek, P.Astakhova, T.Chiu, H.-J.Clayton, T.Deller, M.C.Duan, L.Elias, Y.Feuerhelm, J.Grant, J.C.Grzechnik, S.K.Han, G.W.Jaroszewski, L.Jin, K.K.Klock, H.E.Knuth, M.W.K Tags: structural genomics DUFs glycolipids osmotic stress host – pathogen interactions structural communications Source Type: journals

Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolismEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel α+β fold comprising two β-sheets packed against a single helix. A remote structural similarity to two other uncharacterized protein families specific to the Bacillus genus (PF08868 and PF08968), as well as to prokaryotic S-adenosylmethionine decarboxylases, is consistent with a role in amino-acid metabolism. Genomic neighborhood analysis of LP2179 supports this functional assignment, which might also then be extended to PF08868 and PF08968. (Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - October 27, 2009 Category: Biochemistry Authors: Bakolitsa, C.Kumar, A.Carlton, D.Miller, M.D.Krishna, S.S.Abdubek, P.Astakhova, T.Axelrod, H.L.Chiu, H.-J.Clayton, T.Deller, M.C.Duan, L.Elsliger, M.-A.Feuerhelm, J.Grzechnik, S.K.Grant, J.C.Han, G.W.Jaroszewski, L.Jin, K.K.Klock, H.E.Knuth, M.W.Kozbial, Tags: structural genomics DUFs S-adenosylmethionine decarboxylase amino-acid metabolism probiotics structural communications Source Type: journals

The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 Å resolution reveals a new fold (the ABATE domain) and suggests its possible role as a transcription regulatorEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The crystal structure of Jann_2411 from Jannaschia sp. strain CCS1, a member of the Pfam PF07336 family classified as a domain of unknown function (DUF1470), was solved to a resolution of 1.45 Å by multiple-wavelength anomalous dispersion (MAD). This protein is the first structural representative of the DUF1470 Pfam family. Structural analysis revealed a two-domain organization, with the N-terminal domain presenting a new fold called the ABATE domain that may bind an as yet unknown ligand. The C-terminal domain forms a treble-clef zinc finger that is likely to be involved in DNA binding. Analysis of the Jann_2411 prote...
Source: Acta Crystallographica Section F - October 27, 2009 Category: Biochemistry Authors: Bakolitsa, C.Bateman, A.Jin, K.K.McMullan, D.Krishna, S.S.Miller, M.D.Abdubek, P.Acosta, C.Astakhova, T.Axelrod, H.L.Burra, P.Carlton, D.Chiu, H.-J.Clayton, T.Das, D.Deller, M.C.Duan, L.Elias, Y.Feuerhelm, J.Grant, J.C.Grzechnik, A.Grzechnik, S.K.Han, G.W Tags: structural genomics environmental stress domains of unknown function Pfam bound metal identification structural communications Source Type: journals

Structures of BIR domains from human NAIP and cIAP2Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The inhibitor of apoptosis (IAP) family of proteins contains key modulators of apoptosis and inflammation that interact with caspases through baculovirus IAP-repeat (BIR) domains. Overexpression of IAP proteins frequently occurs in cancer cells, thus counteracting the activated apoptotic program. The IAP proteins have therefore emerged as promising targets for cancer therapy. In this work, X-ray crystallography was used to determine the first structures of BIR domains from human NAIP and cIAP2. Both structures harbour an N-terminal tetrapeptide in the conserved peptide-binding groove. The structures reveal that these two p...
Source: Acta Crystallographica Section F - October 23, 2009 Category: Biochemistry Authors: Herman, M.D.Moche, M.Flodin, S.Welin, M.Trésaugues, L.Johansson, I.Nilsson, M.Nordlund, P.Nyman, T. Tags: apoptosis cancer inflammation IAP NAIP cIAP BIR structural communications Source Type: journals

Structure of an Escherichia coli N-acetyl-d-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 Å resolutionEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The structure of a mutant variant of Escherichia coli N-acetyl-d-neuraminic acid lyase (NAL), E192N, in complex with pyruvate has been determined in a new crystal form. It crystallized in space group P212121, with unit-cell parameters a = 78.3, b = 108.5, c = 148.3 Å. Pyruvate has been trapped in the active site as a Schiff base with the catalytic lysine (Lys165) without the need for reduction. Unlike the previously published crystallization conditions for the wild-type enzyme, in which a mother-liquor-derived sulfate ion is strongly bound in the catalytic pocket, the low-salt conditions described here will facilitate...
Source: Acta Crystallographica Section F - October 23, 2009 Category: Biochemistry Authors: Campeotto, I.Carr, S.B.Trinh, C.H.Nelson, A.S.Berry, A.Phillips, S.E.V.Pearson, A.R. Tags: N-acetyl-d-neuraminic acid lyase directed evolution Schiff base aldolases structural communications Source Type: journals

The 1.9 Å structure of the branched-chain amino-acid transaminase (IlvE) from Mycobacterium tuberculosisEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Unlike mammals, bacteria encode enzymes that synthesize branched-chain amino acids. The pyridoxal 5′-phosphate-dependent transaminase performs the final biosynthetic step in these pathways, converting keto acid precursors into α-amino acids. The branched-chain amino-acid transaminase from Mycobacterium tuberculosis (MtIlvE) has been crystallized and its structure has been solved at 1.9 Å resolution. The MtIlvE monomer is composed of two domains that interact to form the active site. The biologically active form of IlvE is a homodimer in which each monomer contributes a substrate-specificity loop to the partner molec...
Source: Acta Crystallographica Section F - October 13, 2009 Category: Biochemistry Authors: Tremblay, L.W.Blanchard, J.S. Tags: Mycobacterium tuberculosis transaminases pyridoxal 5 ′ -phosphate pyridoxamine 5 branched-chain amino acids structural communications Source Type: journals

Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radioduransEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Nudix pyrophosphatases are a well represented protein family in the Deinococcus radiodurans genome. These hydrolases, which are known to be enzymatically active towards nucleoside diphosphate derivatives, play a role in cleansing the cell pool of potentially deleterious damage products. Here, the structure of DR2204, the only ADP-ribose pyrophosphatase in the D. radiodurans genome that is known to be active towards flavin adenosine dinucleotide (FAD), is presented at 2.0 Å resolution. (Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - October 12, 2009 Category: Biochemistry Authors: Gonçalves, A.M.D.Fioravanti, E.Stelter, M.McSweeney, S. Tags: ADP-ribose pyrophosphatases Deinococcus radiodurans structural communications Source Type: journals

Structure of the adenylation domain of NAD+-dependent DNA ligase from Staphylococcus aureusEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
DNA ligase catalyzes phosphodiester-bond formation between immediately adjacent 5′-phosphate and 3′-hydroxyl groups in double-stranded DNA and plays a central role in many cellular and biochemical processes, including DNA replication, repair and recombination. Bacterial NAD+-dependent DNA ligases have been extensively characterized as potential antibacterial targets because of their essentiality and their structural distinction from human ATP-dependent DNA ligases. The high-resolution structure of the adenylation domain of Staphylococcus aureus NAD+-dependent DNA ligase establishes the conserved domain architecture wit...
Source: Acta Crystallographica Section F - October 12, 2009 Category: Biochemistry Authors: Han, S.Chang, J.S.Griffor, M. Tags: NAD NMN NAD -dependent DNA ligases structural communications Source Type: journals

Laboratory Communications in Acta Crystallographica Section FEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
(Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - September 29, 2009 Category: Biochemistry Authors: Weiss, M.S.Einspahr, H. Tags: Editorial Source Type: journals

How to get the magic triangle and the MAD triangle into your protein crystalEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The magic triangle 5-amino-2,4,6-triiodoisophthalic acid (I3C) and the MAD triangle 5-amino-2,4,6-tribromoisophthalic acid (B3C) are two representatives of a novel class of compounds that combine heavy atoms for experimental phasing with functional groups for protein interactions. These compounds are readily available and provide easy access to experimental phasing. The preparation of stock solutions and the incorporation of the compounds into protein crystals are discussed. As an example of incorporation via cocrystallization, the incorporation of B3C into bovine trypsin, resulting in a single site with high occupancy, i...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Beck, T.da Cunha, C.E.Sheldrick, G.M. Tags: phasing tools incorporation soaking cocrystallization experimental phasing laboratory communications Source Type: journals

Cloning, purification and preliminary X-ray crystallographic analysis of a hypothetical protein, MJ0754, from Methanococcus jannaschii DSM 2661Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The protein encoded by the MJ0754 gene from the archaeon Methanococcus jannaschii DSM 2661 is an unknown hypothetical protein. Two recombinant proteins, MJ0754 (residues 1–185) and MJ0754t (a truncated form of MJ0754, residues 11–185), were cloned from MJ0754, overexpressed as His-tag fusion proteins and purified. The crystals were found to grow under two different conditions and to have two different shapes. The crystal of MJ0754 belonged to space group P61, with unit-cell parameters a = b = 127.015, c = 48.929 Å, a calculated Matthews coefficient of 2.85 Å3 Da−1 and two molecules per asymmetric unit. The cr...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Lee, E.H.Nam, K.H.Hwang, K.Y. Tags: MJ0754 Methanococcus jannaschii hypothetical proteins ferritin-like diiron-carboxylate proteins crystallization communications Source Type: journals

Crystallization and preliminary X-ray diffraction analysis of the middle domain of Paip1Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The poly(A)-binding protein (PABP) simultaneously interacts with the poly(A) tail of mRNAs and the scaffolding protein eIF4G to mediate mRNA circularization, resulting in stimulation of protein translation. PABP is regulated by the PABP-interacting protein Paip1. Paip1 is thought to act as a translational activator in 5′ cap-dependent translation by interacting with PABP and the initiation factors eIF4A and eIF3. Here, the crystallization and preliminary diffraction analysis of the middle domain of Paip1 (Paip1M), which produces crystals that diffract to a resolution of 2.2 Å, are presented. (Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Kanaan, A.S.Frank, F.Maedler-Kron, C.Verma, K.Sonenberg, N.Nagar, B. Tags: Paip1 PABP eIF3 eIF4A eIF4G initiation factors eIFs mRNA translation translational stimulation crystallization communications Source Type: journals

Crystallization and preliminary X-ray diffraction characterization of an essential protein from Xanthomonas campestris that contains a noncanonical PilZ signature motif yet is critical for pathogenicityEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Recent studies have identified c-di-GMP as a novel secondary messenger molecule that is heavily involved in regulating bacterial biofilm formation, motility, production of pathogenicity factors etc. PilZ domain-containing proteins have been suggested and subsequently proved to be the c-di-GMP receptor. However, considering the diverse biological functions exhibited by c-di-GMP, it may be that receptors other than the PilZ domain exist. An essential protein from the plant pathogen Xanthomonas campestris pv. campestris (Xcc) that contains a noncanonical PilZ signature motif yet is critical for Xcc pathogenicity has been clon...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Li, T.-N.Chin, K.-H.Shih, H.-L.Wang, A.H.-J.Chou, S.-H. Tags: c-di-GMP PilZ Xanthomonous campestris crystallization communications Source Type: journals

Preliminary X-ray crystallographic analysis of a nitric oxide-inducible lactate dehydrogenase from Staphylococcus aureusEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Recent studies have indicated that Staphylococcus aureus can survive the nitrosative stress (caused by the radical nitric oxide; NO·) mounted by the immune system of the infected host. It does this by expressing a nitric oxide-inducible l-lactate dehydrogenase (Sa-LDH-1). Therefore, if efficient inhibitors of Sa-LDH-1 can be designed then Sa-LDH-1 could be a potential drug target against the pathogen S. aureus. For this purpose, the nitric acid-inducible LDH-1 from S. aureus COL strain has been cloned into the expression vector pET-28a(+) and the protein has been expressed, purified and crystallized. The Sa-LDH-1 crystal...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Dong, J.-B.Liu, X.Li, L.-F.Wu, S.Su, X.-D. Tags: nitric oxide-inducible lactate dehydrogenase Staphylococcus aureus crystallization communications Source Type: journals

A novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis: protein purification, crystallization and X-ray diffraction analysisEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Chorismate mutase catalyzes a key step in the shikimate-biosynthetic pathway and hence is an essential enzyme in bacteria, plants and fungi. Mycobacterium tuberculosis contains two chorismate mutases, a secreted and an intracellular one, the latter of which (MtCM; Rv0948c; 90 amino-acid residues; 10 kDa) is the subject of this work. Here are reported the gene expression, purification and crystallization of MtCM alone and of its complex with another shikimate-pathway enzyme, DAHP synthase (MtDS; Rv2178c; 472 amino-acid residues; 52 kDa), which has been shown to enhance the catalytic efficiency of MtCM. The MtCM–MtDS c...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Ökvist, M.Sasso, S.Roderer, K.Kast, P.Krengel, U. Tags: AroQ chorismate mutase drug targets enzyme catalysis multi-enzyme complexes Mycobacterium tuberculosis Rv0948c noncovalent protein complexes shikimate pathway transition-state analogues crystallization communications Source Type: journals

Towards the structure of the C-terminal part of the S-layer protein SbsCEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The S-layer protein SbsC from Geobacillus stearothermophilus ATCC 12980 is the most prevalent single protein produced by the bacterium and covers the complete bacterial surface in the form of a two-dimensional crystalline monolayer. In order to elucidate the structural features of the assembly domains, several N-terminally truncated fragments of SbsC have been crystallized. Crystals obtained from recombinant fragments showed anisotropic diffraction to a maximum of 3.5 Å resolution using synchrotron radiation. The best diffracting crystals were obtained from rSbsC(755–1099), an unintentional in situ proteolytic degrada...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Kroutil, M.Pavkov, T.Birner-Gruenberger, R.Tesarz, M.Sleytr, U.B.Egelseer, E.M.Keller, W. Tags: S-layer proteins SbsC crystallization communications Source Type: journals

Crystallization and preliminary X-ray crystallographic studies of O-methyltransferase from Anabaena PCC 7120Email this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
O-Methyltransferase (OMT) is a ubiquitous enzyme that exists in bacteria, plants and humans and catalyzes a methyl-transfer reaction using S-adenosyl-l-methionine as a methyl donor and a wide range of phenolics as acceptors. To investigate the structure and function of OMTs, omt from Anabaena PCC 7120 was cloned into expression vector pET21a and expressed in a soluble form in Escherichia coli strain BL21 (DE3). The recombinant OMT protein was purified to homogeneity using a two-step strategy. Crystals of OMT that diffracted to a resolution of 2.4 Å were obtained using the hanging-drop vapour-diffusion method. The crysta...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Li, G.Tang, Z.Meng, G.Dai, K.Zhao, J.Zheng, X. Tags: O-methyltransferases Anabaena PCC 7120 crystallization communications Source Type: journals

Expression, purification and preliminary crystallographic analysis of Pseudomonas aeruginosa RocR proteinEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Pseudomonas aeruginosa RocR, an EAL-domain protein which regulates the expression of virulence genes and biofilm formation, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of RocR are reported. The X-ray diffraction data were processed to a resolution of 2.50 Å. The crystals belonged to space group P6122 or P6522, with unit-cell parameters a = 118.8, b = 118.8, c = 495.1 Å, α = β = 90, γ = 120°. (Source: Acta Crystallographica Section F)
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Kotaka, M.Dutta, S.Lee, H.C.Lim, M.J.M.Wong, Y.Rao, F.Mitchell, E.P.Liang, Z.-X.Lescar, J. Tags: RocR EAL-domain proteins Pseudomonas aeruginosa crystallization communications Source Type: journals

Crystallization and crystal-packing studies of Chlorella virus deoxyuridine triphosphataseEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The 141-amino-acid deoxyuridine triphosphatase (dUTPase) from the algal Chlorella virus IL-3A and its Glu81Ser/Thr84Arg-mutant derivative Mu-22 were crystallized using the hanging-drop vapor-diffusion method at 298 K with polyethylene glycol as the precipitant. An apo IL-3A dUTPase with an amino-terminal T7 epitope tag and a carboxy-terminal histidine tag yielded cubic P213 crystals with unit-cell parameter a = 106.65 Å. In the presence of dUDP, the enzyme produced thin stacked orthorhombic P222 crystals with unit-cell parameters a = 81.0, b = 96.2, c = 132.8 Å. T7-histidine-tagged Mu-22 dUTPase formed thin stacked...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Homma, K.Moriyama, H. Tags: Chlorella virus dUTPases crystallization communications Source Type: journals

High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug designEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
The crystal structure of human carbonic anhydrase II (CA II) complexed with the inhibitor acetazolamide (AZM) has been determined at 1.1 Å resolution and refined to an Rcryst of 11.2% and an Rfree of 14.7%. As observed in previous CA II–inhibitor complexes, AZM binds directly to the zinc and makes several key interactions with active-site residues. The high-resolution data also showed a glycerol molecule adjacent to the AZM in the active site and two additional AZMs that are adventitiously bound on the surface of the enzyme. The co-binding of AZM and glycerol in the active site demonstrate that given an appropriate ri...
Source: Acta Crystallographica Section F - September 24, 2009 Category: Biochemistry Authors: Sippel, K.H.Robbins, A.H.Domsic, J.Genis, C.Agbandje-McKenna, M.McKenna, R. Tags: human carbonic anhydrase II acetazolamide inhibitor design structural communications Source Type: journals

Purification, crystallization and preliminary X-ray diffraction studies of parakeet (Psittacula krameri) haemoglobinEmail this article to a colleague. Save this article to My Clippings. Discuss or comment on this article.
Birds often show efficient oxygen management in order to meet the special demands of their metabolism. However, the structural studies of avian haemoglobins (Hbs) are inadequate for complete understanding of the mechanism involved. Towards this end, purification, crystallization and preliminary X-ray diffraction studies have been carried out for parakeet Hb. Parakeet Hb was crystallized as the met form in low-salt buffered conditions after extracting haemoglobin from crude blood by microcentrifugation and purifying the sample by column chromatography. Good-quality crystals were grown from 10% PEG 3350 and a crystal diffrac...
Source: Acta Crystallographica Section F - September 22, 2009 Category: Biochemistry Authors: Jaimohan, S.M.Naresh, M.D.Arumugam, V.Mandal, A.B. Tags: avian haemoglobin Psittacula krameri crystallization communications Source Type: journals