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PDB Code (pdb + code)
Selected AbstractsThe three-dimensional structure of MAP kinase p38,: different features of the ATP-binding site in p38, compared with p38,ACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2009Sangita B. Patel The p38 mitogen-activated protein kinases are activated in response to environmental stress and cytokines and play a significant role in transcriptional regulation and inflammatory responses. Of the four p38 isoforms known to date, two (p38, and p38,) have been identified as targets for cytokine-suppressive anti-inflammatory drugs. Recently, it was reported that specific inhibition of the p38, isoform is necessary and sufficient for anti-inflammatory efficacy in vivo, while further inhibition of p38, may not provide any additional benefit. In order to aid the development of p38,-selective compounds, the three-dimensional structure of p38, was determined. To do so, the C162S and C119S,C162S mutants of human MAP kinase p38, were cloned, expressed in Escherichia coli and purified. Initial screening hits in crystallization trials in the presence of an inhibitor led upon optimization to crystals that diffracted to 2.05,Å resolution and allowed structure determination (PDB codes 3gc8 and 3gc9 for the single and double mutant, respectively). The structure of the p38, C162S mutant in complex with the same inhibitor is also reported (PDB code 3gc7). A comparison between the structures of the two kinases showed that they are highly similar overall but that there are differences in the relative orientation of the N- and C-terminal domains that causes a reduction in the size of the ATP-binding pocket in p38,. This difference in size between the two pockets could be exploited in order to achieve selectivity. [source] What can we learn by computing 13C, chemical shifts for X-ray protein models?ACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2009Yelena A. Arnautova The room-temperature X-ray structures of ubiquitin (PDB code 1ubq) and of the RNA-binding domain of nonstructural protein 1 of influenza A virus (PDB code 1ail) solved at 1.8 and 1.9,Å resolution, respectively, were used to investigate whether a set of conformations rather than a single X-ray structure provides better agreement with both the X-ray data and the observed 13C, chemical shifts in solution. For this purpose, a set of new conformations for each of these proteins was generated by fitting them to the experimental X-ray data deposited in the PDB. For each of the generated structures, which show R and Rfree factors similar to those of the deposited X-ray structure, the 13C, chemical shifts of all residues in the sequence were computed at the DFT level of theory. The sets of conformations were then evaluated by their ability to reproduce the observed 13C, chemical shifts by using the conformational average root-mean-square-deviation (ca-r.m.s.d.). For ubiquitin, the computed set of conformations is a better representation of the observed 13C, chemical shifts in terms of the ca-r.m.s.d. than a single X-ray-derived structure. However, for the RNA-binding domain of nonstructural protein 1 of influenza A virus, consideration of an ensemble of conformations does not improve the agreement with the observed 13C, chemical shifts. Whether an ensemble of conformations rather than any single structure is a more accurate representation of a protein structure in the crystal as well as of the observed 13C, chemical shifts is determined by the dispersion of coordinates, in terms of the all-atom r.m.s.d. among the generated models; these generated models satisfy the experimental X-ray data with accuracy as good as the PDB structure. Therefore, generation of an ensemble is a necessary step to determine whether or not a single structure is sufficient for an accurate representation of both experimental X-ray data and observed 13C, chemical shifts in solution. [source] Application of molecular replacement to protein powder data from image platesACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2009Jennifer A. Doebbler Macromolecular structures can be solved via molecular replacement from powder diffraction data collected not only on multi-analyzer diffractometers but also on image plates. Diffraction peaks recorded on image plates are generally broader than those collected using an array of crystal analyzer detectors, but the image-plate data often allow the use of powder data to lower d -spacings. Owing to the high incidence of overlaps in powder patterns, which is especially evident for larger structures, a multi-pattern Pawley refinement is necessary in order to distinguish intensity peaks. This work utilized various salt concentrations to produce small lattice distortions, which resulted in shifts of Bragg peak positions, in a suite of five powder patterns. Using reflection structure factors obtained from this combined refinement, the structure of hen egg-white lysozyme was determined by molecular replacement using the 60% identical human lysozyme (PDB code 1lz1) as the search model. This work also expands upon previous work by presenting a full-scale multi-species analysis combined with an investigation of the sensitivity with regard to discrimination between incorrect fold types. To test the limits of this technique, extension to higher molecular-weight structures is ongoing. [source] Structural insight into nucleotide recognition by human death-associated protein kinaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 3 2009Laurie K. McNamara Death-associated protein kinase (DAPK) is a member of the Ca2+/calmodulin-regulated family of serine/threonine protein kinases. The role of the kinase activity of DAPK in eukaryotic cell apoptosis and the ability of bioavailable DAPK inhibitors to rescue neuronal death after brain injury have made it a drug-discovery target for neurodegenerative disorders. In order to understand the recognition of nucleotides by DAPK and to gain insight into DAPK catalysis, the crystal structure of human DAPK was solved in complex with ADP and Mg2+ at 1.85,Å resolution. ADP is a product of the kinase reaction and product release is considered to be the rate-limiting step of protein kinase catalytic cycles. The structure of DAPK,ADP,Mg2+ was compared with a newly determined DAPK,AMP-PNP,Mg2+ structure and the previously determined apo DAPK structure (PDB code 1jks). The comparison shows that nucleotide-induced changes are localized to the glycine-rich loop region of DAPK. [source] Crystallographic evidence for noncoplanar catalytic aspartic acids in plasmepsin II resides in the Protein Data BankACTA CRYSTALLOGRAPHICA SECTION D, Issue 3 2009Arthur H. Robbins The carboxylate atoms of the two catalytic aspartic acid residues in aspartic proteases are nearly coplanar and in the uncomplexed form share an in-plane nucleophilic water molecule that is central to the mechanism of these enzymes. This note reports that while reviewing the electron-density maps derived from the deposited data for uncomplexed plasmepsin II from Plasmodium falciparum [Asojo et al. (2003), J. Mol. Biol.327, 173,181; PDB code 1lf4], it was discovered that the aspartic acid residues in this structure should in fact be distinctly noncoplanar. The crystallographic model from the deposited coordinates has been re-refined against the 1.9,Å resolution published diffraction data to an Rcryst of 21.2% and an Rfree of 22.2%. The catalytic water molecule is present, but the plane of the carboxylate group of Asp214 is rotated by 66° from its original position. [source] An alternate description of two crystal structures of phospholipase A2 from Bungarus caeruleusACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2007Isolde Le Trong Reinterpretations of the space-group symmetry are reported for two crystal structures of phospholipase A2 isoforms (PDB codes 1u4j and 1g2x). The two structures reported in space groups R3 and C2 are isomorphous with a third isoform with space group R32 (PDB code 1fe5). The original structure reports were interpreted in terms of different oligomeric forms of the isoforms, but these conclusions are not supported by the isomorphous structures. [source] Crystallization and preliminary analysis of a water-forming NADH oxidase from Lactobacillus sanfranciscensisACTA CRYSTALLOGRAPHICA SECTION D, Issue 11 2004George T. Lountos Single crystals have been obtained of NADH oxidase (Nox), a flavoenzyme cloned from Lactobacillus sanfranciscensis. The enzyme catalyzes the oxidation of two equivalents of NAD(P)H and reduces one equivalent of oxygen to yield two equivalents of water, without releasing hydrogen peroxide after the reduction of the first equivalent of NAD(P)H. The enzyme crystallizes in space group P212121, with unit-cell parameters a = 59.6, b = 92.6, c = 163.5,Å. The crystals diffract to 1.85,Å resolution using synchrotron radiation. Matthews coefficient calculations suggest the presence of two molecules per asymmetric unit (VM = 2.3,Å3,Da,1, 45.5% solvent content), which has been confirmed by the molecular-replacement solution using a search molecule derived from NADH peroxidase (PDB code 1f8w). [source] Crystallization and preliminary X-ray diffraction analysis of shikimate kinase from Mycobacterium tuberculosis in complex with MgADPACTA CRYSTALLOGRAPHICA SECTION D, Issue 12 2001Yijun Gu Shikimate kinase (SK) from Mycobacterium tuberculosis (Mt) was overexpressed in Escherichia coli, purified and cocrystallized with MgADP in hanging drops using the vapor-diffusion procedure with PEG 4000 and 2-propanol as precipitants at pH 7.5. The crystal of MtSK,MgADP, which diffracted to 2.2,Å resolution, belonged to space group P3221 or P3121, with unit-cell parameters a = b = 64.01, c = 92.41,Å. There was one MtSK molecule in the asymmetric unit. Molecular-replacement trials with the crystal structure of SK from Erwinia chrysanthemi (PDB code 1shk) and adenylate kinase (PDB code 1ake) as search models were not successful. Heavy-atom derivative screening is in progress. [source] Structure of a fibronectin type III-like module from Clostridium thermocellumACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2010Markus Alahuhta The 1.6,Å resolution structure of a fibronectin type III-like module from Clostridium thermocellum (PDB code 3mpc) with two molecules in the asymmetric unit is reported. The crystals used for data collection belonged to space group P212121, with unit-cell parameters a = 35.43, b = 45.73, c = 107.72,Å, and the structure was refined to an R factor of 0.166. Structural comparisons found over 800 similar structures in the Protein Data Bank. The broad range of different proteins or protein domains with high structural similarity makes it especially demanding to classify these proteins. Previous studies of fibronectin type III-like modules have indicated that they might function as ligand-binding modules, as a compact form of peptide linkers or spacers between other domains, as cellulose-disrupting modules or as proteins that help large enzyme complexes remain soluble. [source] Structure of the newly found green turtle egg-white ribonucleaseACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2010Somporn Katekaew Marine green turtle (Chelonia mydas) egg-white ribonuclease (GTRNase) was crystallized from 1.1,M ammonium sulfate pH 5.5 and 30% glycerol using the sitting-drop vapour-diffusion method. The structure of GTRNase has been solved at 1.60,Å resolution by the molecular-replacement technique using a model based on the structure of RNase 5 (murine angiogenin) from Mus musculus (46% identity). The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 86.271, b = 34.174, c = 39.738,Å, , = 90, , = 102, , = 90°. GTRNase consists of three helices and seven ,-strands and displays the ,+, folding topology typical of a member of the RNase A superfamily. Superposition of the C, coordinates of GTRNase and RNase A superfamily members indicates that the overall structure is highly similar to that of angiogenin or RNase 5 from M. musculus (PDB code 2bwl) and RNase A from Bos taurus (PDB code 2blz), with root-mean-square deviations of 3.9 and 2.0,Å, respectively. The catalytic residues are conserved with respect to the RNase A superfamily. The three disulfide bridges observed in the reptilian enzymes are conserved in GTRNase, while one further disulfide bond is required for the structural stability of mammalian RNases. GTRNase is expressed in egg white and the fact that its sequence has the highest similarity to that of snapping turtle pancreatic RNase suggests that the GTRNase secreted from oviduct cells to form egg white is probably the product of the same gene as activated in pancreatic cells. [source] Expression, purification, crystallization and preliminary X-ray analysis of rice (Oryza sativa L.) Os4BGlu12 ,-glucosidaseACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2010Sompong Sansenya Rice (Oryza sativa L.) Os4BGlu12, a glycoside hydrolase family 1 ,-glucosidase (EC 3.2.1.21), was expressed as a fusion protein with an N-terminal thioredoxin/His6 tag in Escherichia coli strain Origami B (DE3) and purified with subsequent removal of the N-terminal tag. Native Os4BGlu12 and its complex with 2,4-dinitrophenyl-2-deoxy-2-fluoro-,- d -glucopyranoside (DNP2FG) were crystallized using 19% polyethylene glycol (3350 or 2000, respectively) in 0.1,M Tris,HCl pH 8.5, 0.16,M NaCl at 288,K. Diffraction data sets for the apo and inhibitor-bound forms were collected to 2.50 and 2.45,Å resolution, respectively. The space group and the unit-cell parameters of the crystal indicated the presence of two molecules per asymmetric unit, with a solvent content of 50%. The structure of Os4BGlu12 was successfully solved in space group P43212 by molecular replacement using the white clover cyanogenic ,-glucosidase structure (PDB code 1cbg) as a search model. [source] Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radioduransACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2009Sarathy Karunan Partha UDP-galactopyranose mutase (UGM) catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose. A UGM,substrate complex from Deinococccus radiodurans has been expressed, purified and crystallized. Crystals were obtained by the microbatch-under-oil method at room temperature. The crystals diffracted to 2.36,Å resolution at the Canadian Light Source The space group was found to be P212121, with unit-cell parameters a = 134.0, b = 176.6, c = 221.6,Å. The initial structure solution was determined by molecular replacement using UGM from Mycobacterium tuberculosis (PDB code 1v0j) as a template model. [source] Comparison of GFL,GFR, complexes: further evidence relating GFL bend angle to RET signallingACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2009Vimal Parkash Glial cell line-derived neurotrophic factor (GDNF) activates the receptor tyrosine kinase RET by binding to the GDNF-family receptor ,1 (GFR,1) and forming the GDNF2,GFR,12,RET2 heterohexamer complex. A previous crystal structure of the GDNF2,GFR,12 complex (PDB code 2v5e) suggested that differences in signalling in GDNF-family ligand (GFL) complexes might arise from differences in the bend angle between the two monomers in the GFL homodimer. Here, a 2.35,Å resolution structure of the GDNF2,GFR,12 complex crystallized with new cell dimensions is reported. The structure was refined to a final R factor of 22.5% (Rfree = 28%). The structures of both biological tetrameric complexes in the asymmetric unit are very similar to 2v5e and different from the artemin,GFR,3 structure, even though there is a small change in the structure of the GDNF. By comparison of all known GDNF and artemin structures, it is concluded that GDNF is more bent and more flexible than artemin and that this may be related to RET signalling. Comparisons also suggest that the differences between artemin and GDNF arise from the increased curvature of the artemin `fingers', which both increases the buried surface area in the monomer,monomer interface and changes the intermonomer bend angle. From sequence comparison, it is suggested that neuturin (the second GFL) adopts an artemin-like conformation, while persephin has a different conformation to the other three. [source] Crystallization and preliminary X-ray diffraction analysis of Q4DV70 from Trypanosoma cruzi, a hypothetical protein with a putative thioredoxin domainACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2009Camila Ramos Dos Santos Q4DV70 is annotated in the Trypanosoma cruzi CL Brener genome as a hypothetical protein with a predicted thioredoxin-like fold, although the catalytic cysteine residues that are conserved in typical oxidoreductases are replaced by serine residues. Gene-expression analysis indicates that this protein is differentially expressed during the T. cruzi life cycle, suggesting that it plays an important role during T. cruzi development. The gene coding for Q4DV70 was cloned and the protein was overexpressed in Escherichia coli with an N-terminal His tag. Purification of Q4DV70 was carried out by affinity and size-exclusion chromatography and the His tag was removed by TEV protease digestion. Crystals of Q4DV70 were grown using the sitting-drop vapour-diffusion method. A diffraction data set was collected to 1.50,Å resolution from a single crystal grown in 25% PEG 1500, 200,mM sodium thiocyanate pH 6.9, 10,mM phenol and 10% ethylene glycol. The crystal belonged to space group P212121, with unit-cell parameters a = 35.04, b = 50.32, c = 61.18,Å. The Q4DV70 structure was solved by molecular replacement using protein disulfide isomerase from yeast (PDB code 2b5e) as a search model. Initial refinement of the model indicated that the solution was correct. These data are being used for refinement of the model of Q4DV70. [source] Expression, purification and preliminary X-ray crystallographic analysis of the human major histocompatibility antigen HLA-B*1402 in complex with a viral peptide and with a self-peptideACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2007Pravin Kumar The product of the human major histocompatibility (HLA) class I allele HLA-B*1402 only differs from that of allele HLA-B*1403 at amino-acid position 156 of the heavy chain (Leu in HLA-B*1402 and Arg in HLA-B*1403). However, both subtypes are known to be differentially associated with the inflammatory rheumatic disease ankylosing spondylitis (AS) in black populations in Cameroon and Togo. HLA-B*1402 is not associated with AS, in contrast to HLA-B*1403, which is associated with this disease in the Togolese population. The products of these alleles can present peptides with Arg at position 2, a feature shared by a small group of other HLA-B antigens, including HLA-B*2705, the prototypical AS-associated subtype. Complexes of HLA-B*1402 with a viral peptide (RRRWRRLTV, termed pLMP2) and a self-peptide (IRAAPPPLF, termed pCatA) were prepared and were crystallized using polyethylene glycol as precipitant. The complexes crystallized in space groups P21 (pLMP2) and P212121 (pCatA) and diffracted synchrotron radiation to 2.55 and 1.86,Å resolution, respectively. Unambiguous solutions for both data sets were obtained by molecular replacement using a peptide-complexed HLA-B*2705 molecule (PDB code 1jge) as a search model. [source] Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ionsACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2007Philip D. Kiser GroEL is a member of the ATP-dependent chaperonin family that promotes the proper folding of many cytosolic bacterial proteins. The structures of GroEL in a variety of different states have been determined using X-ray crystallography and cryo-electron microscopy. In this study, a 3.02,Å crystal structure of the native GroEL complex from Escherichia coli is presented. The complex was purified and crystallized in the absence of potassium ions, which allowed evaluation of the structural changes that may occur in response to cognate potassium-ion binding by comparison to the previously determined wild-type GroEL structure (PDB code 1xck), in which potassium ions were observed in all 14 subunits. In general, the structure is similar to the previously determined wild-type GroEL crystal structure with some differences in regard to temperature-factor distribution. [source] The quaternary structure of the amidase from Geobacillus pallidus RAPc8 is revealed by its crystal packingACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 12 2006Vinod B. Agarkar The amidase from Geobacillus pallidus RAPc8, a moderate thermophile, is a member of the nitrilase enzyme superfamily. It converts amides to the corresponding acids and ammonia and has application as an industrial catalyst. RAPc8 amidase has been cloned and functionally expressed in Escherichia coli and has been purified by heat treatment and a number of chromatographic steps. The enzyme was crystallized using the hanging-drop vapour-diffusion method. Crystals produced in the presence of 1.2,M sodium citrate, 400,mM NaCl, 100,mM sodium acetate pH 5.6 were selected for X-ray diffraction studies. A data set having acceptable statistics to 1.96,Å resolution was collected under cryoconditions using an in-house X-ray source. The space group was determined to be primitive cubic P4232, with unit-cell parameter a = 130.49 (±0.05) Å. The structure was solved by molecular replacement using the backbone of the hypothetical protein PH0642 from Pyrococcus horikoshii (PDB code 1j31) with all non-identical side chains substituted with alanine as a probe. There is one subunit per asymmetric unit. The subunits are packed as trimers of dimers with D3 point-group symmetry around the threefold axis in such a way that the dimer interface seen in the homologues is preserved. [source] Expression, crystallization and preliminary crystallographic analysis of SufE (XAC2355) from Xanthomonas axonopodis pv. citriACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2006Cristiane R. Guzzo Xanthomonas axonopodis pv. citri (Xac) SufE (XAC2355) is a member of a family of bacterial proteins that are conserved in several pathogens and phytopathogens. The Escherichia coli suf operon is involved in iron,sulfur cluster biosynthesis under iron-limitation and stress conditions. It has recently been demonstrated that SufE and SufS form a novel two-component cysteine desulfarase in which SufS catalyses the conversion of l -cysteine to l -alanine, forming a protein-bound persulfide intermediate. The S atom is then transferred to SufE, from which it is subsequently transferred to target molecules or reduced to sulfide in solution. Here, the cloning, expression, crystallization and phase determination of Xac SufE crystals are described. Recombinant SufE was crystallized in space group P212121 and diffracted to 1.9,Å resolution at a synchrotron source. The unit-cell parameters are a = 45.837, b = 58.507, c = 98.951,Å, , = , = , = 90°. The calculated Matthews coefficient indicated the presence of two molecules in the asymmetric unit. Phasing was performed by molecular-replacement using E. coli SufE as a model (PDB code 1mzg) and an interpretable map was obtained. [source] Crystallization and preliminary structure analysis of the blue laccase from the ligninolytic fungus Panus tigrinusACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 2 2005Marta Ferraroni The blue laccase from the white-rot basidiomycete fungus Panus tigrinus, an enzyme involved in lignin biodegradation, has been crystallized. P. tigrinus laccase crystals grew within one week at 296,K using the sitting-drop vapour-diffusion method in 22%(w/v) PEG 4000, 0.2,M CaCl2, 100,mM Tris,HCl pH 7.5. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 54.2, b = 111.6, c = 97.1, , = 97.7°, and contain 46% solvent. A complete native data set was collected to 1.4,Å resolution at the copper edge. Molecular replacement using the Coprinus cinereus laccase structure (PDB code 1hfu) as a starting model was performed and initial electron-density maps revealed the presence of a full complement of copper ions. Model refinement is in progress. The P. tigrinus laccase structural model exhibits the highest resolution available to date and will assist in further elucidation of the catalytic mechanism and electron-transfer processes for this class of enzymes. [source] The three-dimensional structure of MAP kinase p38,: different features of the ATP-binding site in p38, compared with p38,ACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2009Sangita B. Patel The p38 mitogen-activated protein kinases are activated in response to environmental stress and cytokines and play a significant role in transcriptional regulation and inflammatory responses. Of the four p38 isoforms known to date, two (p38, and p38,) have been identified as targets for cytokine-suppressive anti-inflammatory drugs. Recently, it was reported that specific inhibition of the p38, isoform is necessary and sufficient for anti-inflammatory efficacy in vivo, while further inhibition of p38, may not provide any additional benefit. In order to aid the development of p38,-selective compounds, the three-dimensional structure of p38, was determined. To do so, the C162S and C119S,C162S mutants of human MAP kinase p38, were cloned, expressed in Escherichia coli and purified. Initial screening hits in crystallization trials in the presence of an inhibitor led upon optimization to crystals that diffracted to 2.05,Å resolution and allowed structure determination (PDB codes 3gc8 and 3gc9 for the single and double mutant, respectively). The structure of the p38, C162S mutant in complex with the same inhibitor is also reported (PDB code 3gc7). A comparison between the structures of the two kinases showed that they are highly similar overall but that there are differences in the relative orientation of the N- and C-terminal domains that causes a reduction in the size of the ATP-binding pocket in p38,. This difference in size between the two pockets could be exploited in order to achieve selectivity. [source] An alternate description of two crystal structures of phospholipase A2 from Bungarus caeruleusACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2007Isolde Le Trong Reinterpretations of the space-group symmetry are reported for two crystal structures of phospholipase A2 isoforms (PDB codes 1u4j and 1g2x). The two structures reported in space groups R3 and C2 are isomorphous with a third isoform with space group R32 (PDB code 1fe5). The original structure reports were interpreted in terms of different oligomeric forms of the isoforms, but these conclusions are not supported by the isomorphous structures. [source] Preliminary structural characterization of human SOUL, a haem-binding proteinACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2009Filipe Freire Human SOUL (hSOUL) is a 23,kDa haem-binding protein that was first identified as the PP23 protein isolated from human full-term placentas. Here, the overexpression, purification and crystallization of hSOUL are reported. The crystals belonged to space group P6422, with unit-cell parameters a = b = 145, c = 60,Å and one protein molecule in the asymmetric unit. X-ray diffraction data were collected to 3.5,Å resolution at the ESRF. A preliminary model of the three-dimensional structure of hSOUL was obtained by molecular replacement using the structures of murine p22HBP (PDB codes 2gov and 2hva), obtained by solution NMR, as search models. [source] | ||||||||||