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Orthorhombic Space Group P212121 (orthorhombic + space_group_p212121)
Selected AbstractsSynthesis, growth and characterization of single crystals of pure and thiourea doped L-glutamic acid hydrochlorideCRYSTAL RESEARCH AND TECHNOLOGY, Issue 1 2007R. Sathyalakshmi Abstract L(+)Glutamic acid hydrochloride [HOOC (CH2)2CH(NH2) COOH·HCl], a monoamino dicarboxylic acid salt of L-Glutamic acid was synthesized and the synthesis was confirmed by FTIR analysis. Solubility of the material in water was determined. Pure and Thiourea doped L-Glutamic acid hydrochloride crystals were grown by low temperature solution growth using solvent evaporation technique. XRD, UV-Vis-NIR analyses were carried out for both pure and thiourea doped crystals. The crystals were qualitatively analyzed by EDAX analysis and the presence of thiourea was confirmed. The cell parameters of L-Glutamic acid hydrochloride have been determined as a = 5.151 Å, b = 11.79 Å, c = 13.35 Å by X-ray diffraction analysis and it crystallizes in orthorhombic space group P212121. UV-Vis-NIR spectra analysis showed good optical transmission in the entire visible region for both pure and doped crystals. Micro hardness of both pure and doped crystals has been determined using Vickers micro hardness tester. The SHG efficiencies of both pure and doped crystals were determined using Kurtz powder test and pure L-Glutamic acid hydrochloride crystal was found to possess better efficiency than thiourea doped L-Glutamic acid hydrochloride crystals. (© 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Structure, growth and optical properties of Zn0.24Ni0.76(SO4)·7H2O single crystalCRYSTAL RESEARCH AND TECHNOLOGY, Issue 9 2004Xinxin Zhuang Abstract A new crystalline complex zinc nickel sulfate heptahydrate (ZNSH) has been prepared. The crystal structure was investigated by x-ray single crystal diffraction method and the empirical formula is Zn0.24Ni0.76(SO4)·7H2O. The ZNSH crystal belongs to the orthorhombic space group P212121 with cell parameters a = 6.7742(14) Å, b = 11.748(2) Å, c = 12.009(2) Å. The deep-green ZNSH single crystal with dimension of 30 × 25 × 25 mm3 has been grown by the cooling solution method. The constituent ratio of ZNSH crystal grown from various compounding solutions at temperature range 40-50 °C is approximate invariant. The crystal absorption spectra with theoretical analysis are reported. (© 2004 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Comparison of the three-dimensional structures of a human Bence-Jones dimer crystallized on Earth and aboard US Space Shuttle Mission STS-95,JOURNAL OF MOLECULAR RECOGNITION, Issue 2 2003Simon S. Terzyan Abstract Crystals of a human (Sea) Bence-Jones dimer were produced in a capillary by vapor diffusion under microgravity conditions in the 9 day US Space Shuttle Mission STS-95. In comparison to ground-based experiments, nucleation was facile and spontaneous in space. Appearance of a very large (8,×,1.6,×,1.0,mm) crystal in a short time period is a strong endorsement for the use of microgravity to produce crystals sufficiently large for neutron diffraction studies. The Sea dimer crystallized in the orthorhombic space group P212121, with a,=,48.9,Å, b,=,85.2,Å, and c,=,114.0,Å. The crystals grown in microgravity exhibited significantly lower mosaicities than those of ground-based crystals and the X-ray diffraction data had a lower overall B factor. Three-dimensional structures determined by X-ray analysis at two temperatures (100 and 293,K) were indistinguishable from those obtained from ground-based crystals. However, both the crystallographic R factor and the free R factor were slightly lower in the models derived from crystals produced in microgravity. The major difference between the two crystal growth systems is a lack of convection and sedimentation in a microgravity environment. This environment resulted in the growth of much larger, higher-quality crystals of the Sea Bence-Jones protein. Structurally, heretofore unrecognized grooves on the external surfaces of the Sea and other immunoglobulin-derived fragments are regular features and may offer supplementary binding regions for super antigens and other elongated ligands in the bloodstream and perivascular tissues. Copyright © 2003 John Wiley & Sons, Ltd. [source] Structural characterization of anhydrous naloxone- and naltrexone hydrochloride by high resolution laboratory X-ray powder diffraction and thermal analysisJOURNAL OF PHARMACEUTICAL SCIENCES, Issue 12 2007Kunihisa Sugimoto Abstract The crystal structures of the analgesic compounds anhydrous naloxone and naltrexone hydrochloride were determined ab initio from high resolution laboratory X-ray powder diffraction data. Both compounds crystallize in the orthorhombic space group P212121 with lattice parameters of a,=,14.6588(10) Å, b,=,17.4363(9) Å, c,=,7.96200(22) Å, and V,=,2035.06(23) Å3 for naloxone hydrochloride and a,=,15.4560(5) Å, b,=,14.9809(4) Å, c,=,7.84121(18) Å, and V,=,1815.58(11) Å3 for naltrexone hydrochloride. The crystal structure of anhydrous naloxone hydrochloride forms one-dimensional chains through hydrogen bonds. In the crystal structure of anhydrous naltrexone hydrochloride, two-dimensional sheets are formed by hydrogen bonds. The dehydration processes of naloxone hydrochloride dehydrate and naltrexone hydrochloride tetrahydrate was analyzed by DTA, DSC, TG, and MG. © 2007 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 96: 3316,3323, 2007 [source] Crystal structure of a dimeric form of streptococcal pyrogenic exotoxin A (SpeA1)PROTEIN SCIENCE, Issue 9 2004Matthew D. Baker Abstract Streptococcal pyrogenic exotoxin A (SpeA1) is a bacterial superantigen associated with scarlet fever and streptococcal toxic shock syndrome (STSS). SpeA1 is found in both monomeric and dimeric forms, and previous work suggested that the dimer results from an intermolecular disulfide bond between the cysteines at positions 90 of each monomer. Here, we present the crystal structure of the dimeric form of SpeA1. The toxin crystallizes in the orthorhombic space group P212121, with two dimers in the crystallographic asymmetric unit. The final structure has a crystallographic R-factor of 21.52% for 7248 protein atoms, 136 water molecules, and 4 zinc atoms (one zinc atom per molecule). The implications of SpeA1 dimer on MHC class II and T-cell receptor recognition are discussed. [source] (S)-Tricarbonyl[(1,2,3,4-,)-(5R,6S)-1-chloro-5,6-dimethoxycyclohexa-1,3-diene]iron(0)ACTA CRYSTALLOGRAPHICA SECTION C, Issue 7 2000Silvia Russi The title compound, [Fe(C8H11ClO2)(CO)3], has been synthesized, isolated and characterized by single-crystal X-ray diffraction. The molecule crystallizes in the orthorhombic space group P212121. The metal,ligand arrangement is typical of (1,3-diene)tricarbonyliron complexes. [source] Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnelsACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2010A. Stsiapanava The haloalkane dehalogenase DhaA from Rhodococcus rhodochrous NCIMB 13064 is a bacterial enzyme that shows catalytic activity for the hydrolytic degradation of the highly toxic industrial pollutant 1,2,3-trichloropropane (TCP). Mutagenesis focused on the access tunnels of DhaA produced protein variants with significantly improved activity towards TCP. Three mutants of DhaA named DhaA04 (C176Y), DhaA14 (I135F) and DhaA15 (C176Y + I135F) were constructed in order to study the functional relevance of the tunnels connecting the buried active site of the protein with the surrounding solvent. All three protein variants were crystallized using the sitting-drop vapour-diffusion technique. The crystals of DhaA04 belonged to the orthorhombic space group P212121, while the crystals of DhaA14 and DhaA15 had triclinic symmetry in space group P1. The crystal structures of DhaA04, DhaA14 and DhaA15 with ligands present in the active site were solved and refined using diffraction data to 1.23, 0.95 and 1.22,Å, resolution, respectively. Structural comparisons of the wild type and the three mutants suggest that the tunnels play a key role in the processes of ligand exchange between the buried active site and the surrounding solvent. [source] Pseudo-merohedral twinning and noncrystallographic symmetry in orthorhombic crystals of SIVmac239 Nef core domain bound to different-length TCR, fragmentsACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2010Walter M. Kim HIV/SIV Nef mediates many cellular processes through interactions with various cytoplasmic and membrane-associated host proteins, including the signalling , subunit of the T-cell receptor (TCR,). Here, the crystallization strategy, methods and refinement procedures used to solve the structures of the core domain of the SIVmac239 isolate of Nef (Nefcore) in complex with two different TCR, fragments are described. The structure of SIVmac239 Nefcore bound to the longer TCR, polypeptide (Leu51,Asp93) was determined to 3.7,Å resolution (Rwork = 28.7%) in the tetragonal space group P43212. The structure of SIVmac239 Nefcore in complex with the shorter TCR, polypeptide (Ala63,Arg80) was determined to 2.05,Å resolution (Rwork = 17.0%), but only after the detection of nearly perfect pseudo-merohedral crystal twinning and proper assignment of the orthorhombic space group P212121. The reduction in crystal space-group symmetry induced by the truncated TCR, polypeptide appears to be caused by the rearrangement of crystal-contact hydrogen-bonding networks and the substitution of crystallographic symmetry operations by similar noncrystallographic symmetry (NCS) operations. The combination of NCS rotations that were nearly parallel to the twin operation (k, h, ,l) and a and b unit-cell parameters that were nearly identical predisposed the P212121 crystal form to pseudo-merohedral twinning. [source] Structure of a bovine secretory signalling glycoprotein (SPC-40) at 2.1,Å resolutionACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2006Janesh Kumar A recently discovered new class of 40,kDa glycoproteins forms a major component of the secretory proteins in the dry secretions of non-lactating animals. These proteins are implicated as protective signalling factors that determine which cells are to survive during the processes of drastic tissue remodelling. In order to understand its role in the remodelling of mammary glands, the detailed three-dimensional structure of the bovine signalling glycoprotein (SPC-40) has been determined using X-ray crystallography. SPC-40 was purified from bovine dry secretions and crystallized using the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 62.6, b = 67.4, c = 106.9,Å. The protein was also cloned in order to determine its complete amino-acid sequence. Its three-dimensional structure has been determined using data to 2.1,Å resolution. The amino-acid sequence determination of SPC-40 reveals two potential N-glycosylation sites at Asn39 and Asn345, but electron density for a glycan chain was only present at Asn39. The protein adopts a conformation with the classical (,/,)8 -barrel fold of triosephosphate isomerase (TIM barrel; residues 1,237 and 310,360) with the insertion of a small ,+, domain (residues 240,307) similar to that observed in chitinases. However, the substitution of Leu for Glu in the consensus catalytic sequence in SPC-40 caused a loss of chitinase activity. Furthermore, the chitin-binding groove in SPC-40 is considerably distorted owing to unfavourable conformations of several residues, including Trp78, Tyr120, Asp186 and Arg242. Three surface loops, His188,His197, Phe202,Arg212 and Tyr244,Pro260, have exceptionally high B factors, suggesting large-scale flexibility. Fluorescence studies indicate that various sugars bind to SPC-40 with low affinities. [source] Crystallization and preliminary X-ray analysis of heparinase II from Pedobacter heparinusACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2004David Shaya Heparinase II from Pedobacter heparinus (formerly Flavobacterium heparinum), which acts on both heparin and heparan sulfate, is one of several glycosaminoglycan-degrading enzymes produced by this organism. This enzyme, with a molecular weight of 84,kDa, utilizes a lytic mechanism to cleave the ,(1,4) glycosidic bond between hexosamine (d -glucosamine) and l -iduronic or d -glucuronic acid, resulting in a product with an unsaturated sugar ring at the non-reducing end. The enzyme was crystallized by the hanging-drop vapour-diffusion method. The crystals belong to orthorhombic space group P212121 and diffract to 2,Å resolution. There are two molecules in the asymmetric unit, consistent with the finding that recombinant heparinase II functions as a dimer in solution. [source] Characterization, crystallization and preliminary X-ray analysis of bifunctional dihydrofolate reductase,thymidylate synthase from Plasmodium falciparumACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2004Penchit Chitnumsub The full-length pfdhfr-ts genes of the wild-type TM4/8.2 and the double mutant K1CB1 (C59R+S108N) from the genomic DNA of the corresponding Plasmodium falciparum parasite have been cloned into a modified pET(17b) plasmid and expressed in Escherichia coli BL21 (DE3) pLysS. Conditions for the expression and purification of the P. falciparum dihydrofolate reductase,thymidylate synthase (PfDHFR-TS) have been established that yield ,1,mg of the soluble active enzyme per litre of culture. The purified enzymes have been crystallized using a modified microbatch method with PEG 4000 as the primary precipitating agent. X-ray diffraction data were collected to 2.50 and 2.64,Å resolution under cryogenic conditions from single crystals of the two PfDHFR-TS proteins in complex with NADPH, dUMP and either Pyr30 or Pyr39. Preliminary X-ray analysis indicated that the crystals belong to the orthorhombic space group P212121, with two molecules per asymmetric unit and ,52% solvent content (VM, 2.6,Å3,Da,1). The use of a particular type of baby oil in the microbatch setup appeared to be beneficial to PfDHFR-TS crystallization and a preliminary comparison with another commonly used oil is described. [source] Crystallization and preliminary X-ray analysis of a novel Trichoderma reesei xylanase IV belonging to glycoside hydrolase family 5ACTA CRYSTALLOGRAPHICA SECTION D, Issue 3 2004Tarja Parkkinen Xylanase IV (XYN IV) is a new recently characterized xylanase from Trichoderma reesei. It is able to degrade several different xylans, mainly producing xylose. XYN IV has been crystallized by the hanging-drop vapour-diffusion method, using PEG 6000 as a precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 86.3, b = 137.5, c = 196.1,Å, , = , = , = 90°. Assuming a molecular weight of 50.3,kDa, the VM values indicate there to be four XYN IV monomers in an asymmetric unit and the solvent content of the crystals to be 57%. Based on dynamic light-scattering measurements, XYN IV is a dimer in solution. A native data set to 2.8,Å resolution has been collected at a home laboratory and a data set to 2.2,Å resolution has been collected using synchrotron radiation. [source] Crystallization and preliminary X-ray crystallographic study on a xyloglucan-specific exo-,-glycosidase, oligoxyloglucan reducing-end specific cellobiohydrolaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 10 2003Katsuro Yaoi A novel xyloglucan-specific exo-,-glycosidase, oligoxyloglucan reducing-end specific cellobiohydrolase (OXG-RCBH), recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. OXG-RCBH was crystallized by the hanging-drop vapour-diffusion method with polyethylene glycol 3000 and polyethylene glycol 400,as precipitants. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 61.0, b = 146.9, c = 211.9,Å. The crystals diffract to a resolution of 2.2,Å and are suitable for X-ray structure analysis. [source] Purification, crystallization and preliminary X-ray analysis of Caenorhabditis elegans ubiquitin-conjugation enzyme M7.1ACTA CRYSTALLOGRAPHICA SECTION D, Issue 3 2003José A. Gavira M7.1 is a class IV ubiquitin-conjugation enzyme (UBC) that belongs to the ubiquitination cascade in Caenorhabditis elegans. The clone for this UBC has been overexpressed in Escherichia coli and the 16.7,kDa protein was purified from the soluble fraction. M7.1 was crystallized by sitting-drop vapor diffusion in 10% ethanol, 1.5,M NaCl at 277.5,K. Crystals diffracted to 1.75,Å and belong to the orthorhombic space group P212121, with unit-cell parameters a = 44.3, b = 54.3, c = 60.2,Å. The asymmetric unit contains a single monomer. A molecular-replacement model has been determined and refinement is in progress. [source] Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Pseudomonas aeruginosaACTA CRYSTALLOGRAPHICA SECTION D, Issue 10-2 2002Hyung-Wook Kim Peptide deformylase (PDF) from the pathogenic bacterium Pseudomonas aeruginosa has been overexpressed in Escherichia coli and crystallized in the presence of its inhibitor actinonin at 297,K using polyethylene glycol (PEG) 4000 as a precipitant. The diffraction limit and the spot shape of the crystals could be slightly improved by the crystal annealing/dehydration procedure. X-ray diffraction data to 1.85,Å have been collected using synchrotron radiation. The crystal belongs to the orthorhombic space group P212121, with unit-cell parameters a = 68.75, b = 74.46, c = 77.18,Å. The asymmetric unit contains two subunits of peptide deformylase, with a corresponding crystal volume per protein mass (VM) of 2.45,Å3,Da,1 and a solvent content of 49.8%. [source] Purification, crystallization and preliminary X-ray diffraction analysis of yeast nucleosome-assembly factor Cia1pACTA CRYSTALLOGRAPHICA SECTION D, Issue 10-2 2002Balasundaram Padmanabhan Yeast Cia1p is a homologue of human CIA (CCG1-interacting factor A), which possesses nucleosome-assembly activity and interacts with the human TFIID subunit CCG1 and the C-terminal domain of histone H3. The yeast Cia1p without the C-terminal polyanionic stretch has been expressed in Escherichia coli, purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as precipitant. The protein was crystallized in orthorhombic space group P212121, with unit-cell parameters a = 106.70, b = 46.92, c = 40.60,Å and one molecule in the asymmetric unit. The crystal diffracted beyond 2.95,Å resolution using synchrotron radiation. [source] Structure of cytochrome c2 from Rhodospirillum centenumACTA CRYSTALLOGRAPHICA SECTION D, Issue 11 2001A. Camara-Artigas Cytochrome c2 from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 29.7, b = 59.9, c = 65.4,Å, and diffract to a resolution limit of 1.7,Å. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended ,-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed. [source] Crystallization and preliminary X-ray analysis of a thermoalkalophilic lipase from Bacillus stearothermophilus L1ACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2001Seong-Tae Jeong A thermoalkalophilic lipase from Bacillus stearothermophilus L1 (L1 lipase) was crystallized in two different crystal forms using a low concentration of the enzyme and a calcium-exchange process. The first, needle-like, crystal form, which diffracts to about 3.5,Å, belongs to the orthorhombic space group P212121, with unit-cell parameters a = 67.84, b = 72.96, c = 104.41,Å. The second, monoclinic, crystal form, which behaves better than the first form for crystallographic analyses, belongs to the monoclinic space group C2 and has unit-cell parameters a = 119.62, b = 85.05, c = 98.36,Å, , = 99.73°. From the monoclinic crystals, a native data set and a samarium-derivative data set were collected to 2.0 and 2.3,Å resolution, respectively. The difference Patterson map between the two data sets shows strong heavy-atom peaks, indicating that the crystals are suitable for a high-resolution structure determination. [source] A novel 40,kDa protein from goat mammary secretions: purification, crystallization and preliminary X-ray diffraction studiesACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2001P. Kumar A novel 40,kDa protein has been purified from dry secretions of the mammary gland of goats. The first 15 N-terminal residues were sequenced and showed a sequence identity of 30% to a novel 39,kDa whey protein from bovine mammary secretions. The protein was crystallized by the microdialysis method. Protein was dissolved to a concentration of 40,mg,ml,1 in 0.025,M Tris,HCl pH 8.0 and equilibrated with the same buffer containing 19%(v/v) ethanol. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 66.1, b = 107.8, c = 63.2,Å and one molecule per asymmetric unit. Intensity data were collected to 2.9,Å resolution, with a completeness of 95%. Since no similar model is available in the protein structure database, heavy-atom derivatives have been prepared and three-dimensional structure determination using the isomorphous replacement method is in progress. [source] Crystallization and preliminary X-ray crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Saccharomyces cerevisiaeACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2001Byung Woo Han Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) from Saccharomyces cerevisiae is essential for cell viability. It has been overexpressed in Escherichia coli and has been crystallized at 296,K using polyethylene glycol (PEG) 1500 as a precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 59.48, b = 138.54, c = 157.91,Å, , = , = , = 90°. Two molecules of trimeric dUTPase from S. cerevisiae are present in the asymmetric unit, giving a crystal volume per protein mass (VM) of 3.36,Å3,Da,1 and a solvent content of 63%. The diffraction limit of the crystals could be significantly extended by the crystal-annealing procedure. A set of native data extending to 2.7,Å resolution has been collected at 100,K using synchrotron X-rays. [source] Crystallization of Clonorchis sinensis 26,kDa glutathione S-transferase and its fusion proteins with peptides of different lengthsACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2001Young-Hyun Han A Clonorchis sinensis 26,kDa glutathione S-transferase (CsGST) and its fusion proteins containing 14 and 48 amino-acid peptides at the N-terminus have been crystallized using polyethylene glycol monomethylether 550 as a precipitant. Crystals of the three proteins show very similar crystal properties: they diffract to at least 2.3,Å resolution and belong to the orthorhombic space group P212121. The unit-cell parameters of CsGST crystals were a = 66.64,(1), b = 68.91,(1), c = 123.41,(2),Å, which are very close to those of the crystals of the two fusion proteins. In addition, CsGST fusion proteins containing varying extents of N-terminal-extended peptides are incorporated into a crystal, indicating that the extended peptides have little effect on crystal packing. These results suggest that the crystallization system of CsGST/peptide fusion protein may be generally applicable to obtain crystals of small peptides. [source] Crystallization and preliminary X-ray diffraction analysis of a rat biliverdin reductaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2000Danyu Sun Biliverdin reductase (BVR) catalyzes the final step of haem degradation and converts biliverdin to bilirubin using NAD(P)H as an electron donor. This paper deals with the first crystallization and preliminary crystallographic study of recombinant rat BVR expressed in Escherichia coli. Crystals of BVR were obtained by the sitting-drop vapour-diffusion method. Using synchrotron radiation at station BL44B2 of SPring-8, Japan, BVR diffraction data were collected to 1.6,Å resolution. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 58.89, b = 70.41, c = 87.76,Å. The complete determination of the crystallographic structure is currently in progress using MAD (multiwavelength anomalous diffraction) data from an Ir-derivative crystal. [source] Crystallization of native and selenomethionyl yeast orotidine 5,-phosphate decarboxylaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2000Brian G. Miller Crystals of the Saccharomyces cerevisiae pyrimidine biosynthetic enzyme orotidine 5,-phosphate decarboxylase (ODCase) were grown by the hanging-drop vapor-diffusion technique at 277,K using polyethylene glycol 4000 as the precipitant. Crystals of native and selenomethionyl ODCase diffract to less than 2.2,Å and belong to the orthorhombic space group P212121, with unit-cell parameters a = 90.1, b = 116.2, c = 117.0,Å. Crystals of ODCase grown in the presence of the postulated transition-state analog inhibitor 6-hydroxyuridine 5,-phosphate (BMP) diffract to less than 2.5,Å and belong to space group P21, with unit-cell parameters a = 79.9, b = 80.0, c = 98.2,Å, , = 108.6°. [source] High-resolution structure of an ,-spectrin SH3-domain mutant with a redesigned hydrophobic coreACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2010Ana Cámara-Artigas The ,-spectrin SH3 domain (Spc-SH3) is a small modular domain which has been broadly used as a model protein in folding studies and these studies have sometimes been supported by structural information obtained from the coordinates of Spc-SH3 mutants. The structure of B5/D48G, a multiple mutant designed to improve the hydrophobic core and as a consequence the protein stability, has been solved at 1,Å resolution. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 24.79, b = 37.23, c = 62.95,Å. This mutant also bears a D48G substitution in the distal loop and this mutation has also been reported to increase the stability of the protein by itself. The structure of the B5/D48G mutant shows a highly packed hydrophobic core and a more ordered distal loop compared with previous Spc-SH3 structures. [source] Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD from Neisseria meningitidisACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2010Ekaterina Sviridova Fe-regulated protein D (FrpD) is a Neisseria meningitidis outer membrane lipoprotein that may be involved in the anchoring of the secreted repeat in toxins (RTX) protein FrpC to the outer bacterial membrane. However, the function and biological roles of the FrpD and FrpC proteins remain unknown. Native and selenomethionine-substituted variants of recombinant FrpD43,271 protein were crystallized using the sitting-drop vapour-diffusion method. Diffraction data were collected to a resolution of 2.25,Å for native FrpD43,271 protein and to a resolution of 2.00,Å for selenomethionine-substituted FrpD43,271 (SeMet FrpD43,271) protein. The crystals of native FrpD43,271 protein belonged to the hexagonal space group P62 or P64, while the crystals of SeMet FrpD43,271 protein belonged to the primitive orthorhombic space group P212121. [source] Crystallization and preliminary X-ray crystallographic studies of omega-transaminase from Vibrio fluvialis JS17ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2010Tae-ho Jang Omega-transaminase (,-TA) catalyzes the transfer of an amino group from a non-,-position amino acid or an amine compound with no carboxylic group to an amino acceptor. ,-TA from Vibrio fluvialis JS17 (,-TAVf) is a novel amine:pyruvate transaminase that is capable of stereoselective transamination of aryl chiral amines. In this study, ,-TAVf was overexpressed in Escherichia coli with engineered C-terminal His tags. ,-TAVf was then purified to homogeneity and crystallized at 292,K. X-ray diffraction data were collected to a resolution of 2.5,Å from a crystal belonging to the orthorhombic space group P212121, with unit-cell parameters a = 78.43, b = 95.95, c = 122.89,Å. [source] Crystallization and preliminary crystallographic analysis of the Magnetospirillum magneticum AMB-1 and M. gryphiswaldense MSR-1 magnetosome-associated proteins MamAACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2010Natalie Zeytuni MamA is a unique magnetosome-associated protein that is predicted to contain six sequential tetratricopeptide-repeat (TPR) motifs. The TPR structural motif serves as a template for protein,protein interactions and mediates the assembly of multi-protein complexes. Here, the crystallization and preliminary X-ray analysis of recombinant and purified Magnetospirillum magneticum and M.,gryphiswaldense MamA are reported for the first time. M. gryphiswaldense MamA,41 crystallized in the tetragonal space group P41212 or P43212, with unit-cell parameters a = b = 58.88, c = 144.09,Å. M. magneticum MamA,41 crystallized in the orthorhombic space group P212121, with unit-cell parameters a = 44.75, b = 76.19, c = 105.05,Å. X-ray diffraction data were collected to resolutions of 2.0 and 1.95,Å, respectively. [source] Crystallization and preliminary X-ray diffraction analysis of the Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase I86A mutantACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2010Carla Protsko The Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase I86A mutant is stereospecific for (R)-alcohols instead of (S)-alcohols. Pyramidal crystals grown in the presence of (R)-phenylethanol via the hanging-drop vapour-diffusion method diffracted to 3.2,Å resolution at the Canadian Light Source. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 80.23, b = 124.90, c = 164.80,Å. The structure was solved by molecular replacement using the structure of T. brockii SADH (PDB entry 1ykf). [source] Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp.ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2010Purified thermostable recombinant L2 lipase from Bacillus sp. L2 was crystallized by the counter-diffusion method using 20% PEG 6000, 50,mM MES pH 6.5 and 50,mM NaCl as precipitant. X-ray diffraction data were collected to 2.7,Å resolution using an in-house Bruker X8 PROTEUM single-crystal diffractometer system. The crystal belonged to the primitive orthorhombic space group P212121, with unit-cell parameters a = 87.44, b = 94.90, c = 126.46,Å. The asymmetric unit contained one single molecule of protein, with a Matthews coefficient (VM) of 2.85,Å3,Da,1 and a solvent content of 57%. [source] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of 2-keto-3-deoxy-6-phosphogluconate aldolase from Zymomonas mobilis ZM4ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2010Ho-Chang Ryu Zymomonas mobilis ZM4 is an organism optimized for ethanol production which uses the Entner,Doudoroff (ED) pathway for the breakdown of glucose. The key enzyme in this process is 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, which produces glyceraldehyde 3-phosphate and pyruvate. In order to provide a molecular background for the KDPG aldolase from this ethanologenic organism (zmKDPG aldolase), the ZMO0997 gene of Z. mobilis ZM4 coding for zmKDPG aldolase was cloned and expressed and the purified protein was crystallized from 25%(w/v) polyethylene glycol 3350 and 0.1,M bis-tris pH 5.5. Diffraction data were collected to 1.8,Å resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 63.7, b = 83.0, c = 117.2,Å. A trimeric zmKDPG aldolase molecule was present in the asymmetric unit, resulting in a crystal volume per unit protein weight of 2.40,Å3,Da,1 and a solvent content of 48%. [source] | ||||||||||