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Orthorhombic Space Group C2221 (orthorhombic + space_group_c2221)
Selected AbstractsCrystal structures of bovine ,-lactoglobulin in the orthorhombic space group C2221FEBS JOURNAL, Issue 2 2001Structural differences between genetic variants A, features of the Tanford transition The crystal structures of ,-lactoglobulin genetic variants A and B have been determined in the orthorhombic space group C2221 (lattice Y) by X-ray diffraction at 2.0 Å and 1.95 Å resolution, respectively. The structural comparison shows that both variants exhibit the open conformation of the EF loop at the pH of crystallization (pH 7.9), in contrast to what has been reported for the same genetic variants at pH 7.1 in the trigonal space group P3221 (lattice Z) [Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N. & Jameson, G.B. (1999) Protein Sci.8, 75,83]. Furthermore, it was found that the stereochemical environment of Tyr42 changes significantly with pH variation between pH 7 and pH 8. This may provide a structural explanation for an as yet unexplained feature of the Tanford transition, namely the increase in exposure of a tyrosine residue. [source] Crystallization and preliminary X-ray diffraction study of mammalian mitochondrial seryl-tRNA synthetaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2004Sarin Chimnaronk The mitochondrial seryl-tRNA synthetase (mt SerRS) from Bos taurus was overexpressed in Escherichia coli and crystallized using the sitting-drop vapour-diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at room temperature. An appropriate concentration of lithium sulfate was critical for crystal nucleation. Crystals diffracted well beyond a resolution of 1.6,Å and were found to belong to the orthorhombic space group C2221, with unit-cell parameters a = 79.89, b = 230.42, c = 135.60,Å. There is one dimer (Mr, 113,kDa) in the asymmetric unit, with a solvent content of 55%. Efforts to solve the phase problem by molecular replacement are under way. [source] Expression, purification, crystallization and preliminary crystallographic analysis of phosphoserine aminotransferase from Bacillus alcalophilusACTA CRYSTALLOGRAPHICA SECTION D, Issue 12 2003Anatoly P. Dubnovitsky Phosphoserine aminotransferase (PSAT; EC 2.6.1.52) from Bacillus alcalophilus, an obligatory alkalophile with optimum growth at pH 10.6, was overexpressed in Escherichia coli, purified and crystallized under two different conditions using the hanging-drop vapour-diffusion method. Crystals were obtained using trisodium citrate dihydrate or PEG 400 as a precipitating agent. Crystals grown in the presence of trisodium citrate belong to the orthorhombic space group C2221, with unit-cell parameters a = 105.6, b = 136.6, c = 152.0,Å, and those grown in the presence of PEG 400 belong to the orthorhombic space group P21212, with unit-cell parameters a = 143.7, b = 84.3, c = 67.4,Å. Complete data sets were collected to 1.7 and 1.6,Å resolution, respectively, at 100,K using synchrotron radiation. Analysis of the structure of B. alcalophilus PSAT may reveal structural features that contribute to enzyme adaptability at high pH values. [source] An orthorhombic form of Escherichia coli aminopeptidase P at 2.4,Å resolutionACTA CRYSTALLOGRAPHICA SECTION D, Issue 5 2003Stephen C. Graham Aminopeptidase P (AMPP) from Escherichia coli cleaves the N-terminal residue from an oligopeptide if the second residue is proline. The active site contains a dinuclear metal centre. Following earlier structural analyses of crystals in space groups P6422 and I4122, the structure of AMPP has been solved and refined in the orthorhombic space group C2221 at 2.4,Å resolution. There are six subunits in the asymmetric unit. These are arranged in two types of tetramer. One tetramer comprises four crystallographically independent subunits, while the other comprises two pairs of subunits related by a crystallographic twofold axis. The final model of 20,994 protein atoms, 1618 water molecules and 12 metal atoms refined to residuals R = 0.195 and Rfree = 0.215. The molecular structure confirms most of the previously reported features, including the subunit,subunit interfaces in the tetramer and persistent disorder at some residues. The metal,ligand bond lengths at the active site suggest that one of the two Mn atoms is five-coordinate rather than six-coordinate. [source] Crystallization and preliminary X-ray diffraction studies of a novel alkaline serine protease (KP-43) from alkaliphilic Bacillus sp. strain KSM-KP43ACTA CRYSTALLOGRAPHICA SECTION D, Issue 5 2001Tsuyoshi Nonaka A novel alkaline serine protease (KP-43) which belongs to a new class of the subtilisin superfamily was crystallized by the sitting-drop vapour-diffusion method with ammonium sulfate as a precipitant. The crystals belong to the orthorhombic space group C2221, with unit-cell parameters a = 43.50,(2), b = 110.4,(1), c = 168.9,(1),Å. The crystals diffract X-rays beyond 1.9,Å resolution using Cu,K, radiation from a rotating-anode generator and are suitable for high-resolution crystal structure analysis. [source] Overexpression, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa MnmE, a GTPase involved in tRNA modificationACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2010Hyung Ho Lee MnmE, an evolutionarily conserved GTPase, is involved in modification of the uridine base (U34) at the wobble position of certain tRNAs. Previous crystal structures of MnmE suggest that it is a dimer with considerable conformational flexibility. To facilitate structural comparisons among MnmE proteins, structural analysis of MnmE from Pseudomonas aeruginosa encoded by the PA5567 gene was initiated. It was overexpressed in Escherichia coli and crystallized at 297,K using a reservoir solution consisting of 100,mM sodium ADA pH 6.5, 12%(w/v) polyethylene glycol 4000, 100,mM lithium sulfate, 2%(v/v) 2-propanol and 2.5,mM dithiothreitol. X-ray diffraction data were collected to 2.69,Å resolution. The crystals belonged to the orthorhombic space group C2221, with unit-cell parameters a = 96.74, b = 204.66, c = 120.90,Å. Two monomers were present in the asymmetric unit, resulting in a crystal volume per protein mass (VM) of 2.99,Å3,Da,1 and a solvent content of 58.8%. [source] Preliminary X-ray crystallographic analysis of SMU.2055 protein from the caries pathogen Streptococcus mutansACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2010Wang-Hong Zhao The SMU.2055 gene from the major caries pathogen Streptococcus mutans is annotated as a putative acetyltransferase with 163 amino-acid residues. In order to identify its function via structural studies, the SMU.2055 gene was cloned into the expression vector pET28a. Native and SeMet-labelled SMU.2055 proteins with a His6 tag at the N-terminus were expressed at a high level in Escherichia coli strain BL21 (DE3) and purified to homogeneity by Ni2+ -chelating affinity chromatography. Diffraction-quality crystals of SeMet-labelled SMU.2055 were obtained using the sitting-drop vapour-diffusion method and diffracted to a resolution of 2.5,Å on beamline BL17A at the Photon Factory, Tsukuba, Japan. The crystals belong to the orthorhombic space group C2221, with unit-cell parameters a = 92.0, b = 95.0, c = 192.2,Å. The asymmetric unit contained four molecules, with a solvent content of 57.1%. [source] Purification, crystallization and preliminary crystallographic studies of a Kunitz-type proteinase inhibitor from tamarind (Tamarindus indica) seedsACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2009Dipak N. Patil A Kunitz-type proteinase inhibitor has been purified from tamarind (Tamarindus indica) seeds. SDS,PAGE analysis of a purified sample showed a homogeneous band corresponding to a molecular weight of 21,kDa. The protein was identified as a Kunitz-type proteinase inhibitor based on N-terminal amino-acid sequence analysis. It was crystallized by the vapour-diffusion method using PEG 6000. The crystals belonged to the orthorhombic space group C2221, with unit-cell parameters a = 37.2, b = 77.1, c = 129.1,Å. Diffraction data were collected to a resolution of 2.7,Å. Preliminary crystallographic analysis indicated the presence of one proteinase inhibitor molecule in the asymmetric unit, with a solvent content of 44%. [source] Crystallization and preliminary crystallographic studies of the recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 12 2006Sergio Martínez-Rodríguez Dihydropyrimidinases are involved in the reductive pathway of pyrimidine degradation, catalysing the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N -carbamoyl ,-amino acids. This enzyme has often been referred to as hydantoinase owing to its industrial application in the production of optically pure amino acids starting from racemic mixtures of 5-monosubstituted hydantoins. Recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114 (SmelDhp) has been expressed, purified and crystallized. Crystallization was performed using the counter-diffusion method with capillaries of 0.3,mm inner diameter. Crystals of SmelDhp suitable for data collection and structure determination were grown in the presence of agarose at 0.1%(w/v) in order to ensure mass transport controlled by diffusion. X-ray data were collected to a resolution of 1.85,Å. The crystal belongs to the orthorhombic space group C2221, with unit-cell parameters a = 124.89, b = 126.28, c = 196.10,Å and two molecules in the asymmetric unit. A molecular-replacement solution has been determined and refinement is in progress. [source] | ||||||||||