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Tetragonal Crystals (tetragonal + crystal)
Terms modified by Tetragonal Crystals Selected AbstractsGd-HPDO3A, a complex to obtain high-phasing-power heavy-atom derivatives for SAD and MAD experiments: results with tetragonal hen egg-white lysozymeACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2002Éric Girard A neutral gadolinium complex, Gd-HPDO3A, is shown to be a good candidate to use to obtain heavy-atom derivatives and solve macromolecular structures using anomalous dispersion. Tetragonal crystals of a gadolinium derivative of hen egg-white lysozyme were obtained by co-crystallization using different concentrations of the complex. Diffraction data from three derivative crystals (100, 50 and 10,mM) were collected to a resolution of 1.7,Å using Cu,K, radiation from a rotating anode. Two strong binding sites of the gadolinium complex to the protein were located from the gadolinium anomalous signal in both the 100 and 50,mM derivatives. A single site is occupied in the 10,mM derivative. Phasing using the anomalous signal at a single wavelength (SAD method) leads to an electron-density map of high quality. The structure of the 100,mM derivative has been refined. Two molecules of the gadolinium complex are close together. Both molecules are located close to tryptophan residues. Four chloride ions were found. The exceptional quality of the SAD electron-density map, only enhanced by solvent flattening, suggests that single-wavelength anomalous scattering with the Gd-HPDO3A complex may be sufficient to solve protein structures of high molecular weight by synchrotron-radiation experiments, if not by laboratory experiments. [source] The coordination polymers poly[,-4,4,-bipyridyl-di-,-formato-copper(II)] and catena -poly[[[diaqua(1-benzofuran-2,3-dicarboxylato)copper(II)]-,-1,2-di-4-pyridylethane] dihydrate]ACTA CRYSTALLOGRAPHICA SECTION C, Issue 5 2009Rajesh Koner The title compounds, [Cu(CHO2)2(C10H8N2)]n, (I), and {[Cu(C10H4O5)(C12H12N2)(H2O)2]·2H2O}n, (II), are composed of one-dimensional linear coordination polymers involving copper(II) ions and bidentate bipyridyl species. In (I), the polymeric chains are located on twofold rotation axes at (x, x, 0) and are arranged in layered zones centered at z = 0, , ½ and parallel to the ab plane of the tetragonal crystal. Weak coordination of the formate anions of one layer to the copper centers of neighboring layers imparts a three-dimensional connectivity to this structure. In (II), the polymeric chains propagate parallel to the a axis of the crystal. Noncoordinated water molecules link the chains through O,H...O hydrogen bonding in directions perpendicular to c, imparting to the entire structure three-dimensional connectivity. The metal ions adopt distorted octahedral and square-based pyramidal environments in (I) and (II), respectively. This study indicates that, under the given conditions, extended coordination involves CuII centers associating with the bipyridyl ligands rather than with the competing benzofurandicarboxylate entities. [source] Cryoprotection properties of salts of organic acids: a case study for a tetragonal crystal of HEW lysozymeACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2010Grzegorz Bujacz Currently, the great majority of the data that are used for solving macromolecular structures by X-ray crystallography are collected at cryogenic temperatures. Selection of a suitable cryoprotectant, which ensures crystal stability at low temperatures, is critical for the success of a particular diffraction experiment. The effectiveness of salts of organic acids as potential cryoprotective agents is presented in the following work. Sodium formate, acetate, malonate and citrate were tested, as were sodium potassium tartrate and acetate in the form of potassium and ammonium salts. For each salt investigated, the minimal concentration that was required for successful cryoprotection was determined over the pH range 4.5,9.5. The cryoprotective ability of these organic salts depends upon the number of carboxylic groups; the lowest concentration required for cryoprotection was observed at neutral pH. Case-study experiments conducted using the tetragonal form of hen egg-white lysozyme (HEWL) confirmed that salts of organic acids can successfully act as cryoprotective agents of protein crystals grown from high concentrations of inorganic salts. When crystals are grown from solutions containing a sufficient concentration of organic acid salts no additional cryoprotection is needed as the crystals can safely be frozen directly from the crystallizing buffers. [source] Crystallization and preliminary crystallographic data of a leucotoxin S component from Staphylococcus aureusACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2004Valérie Guillet Class S proteins of staphylococcal bicomponent pore-forming leucotoxins play an important role in membrane targetting and cell specificity. Wild-type and recombinant S components of the Panton,Valentine leucocidin (LukS-PV) were expressed in Staphylococcus aureus and Escherichia coli, respectively, and purified. Both proteins were crystallized in two crystal forms with Jeffamine M-600 as the precipitant at 285,K using the hanging-drop vapour-diffusion method and seeding techniques. Crystals belong to space group P2 (or P21) and P41 (or P43), with unit-cell parameters a = 72.3, b = 95.1, c = 108.1,Å, , = 106.4° and a = b = 94.8, c = 306.2,Å, respectively. A full set of X-ray diffraction data was collected to 2.1,Å from a single tetragonal crystal of the wild-type protein at 100,K. [source] Structure of tetragonal crystals of human erythrocyte catalaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2001Martin K. Safo The structure of catalase from human erythrocytes (HEC) was determined in tetragonal crystals of space group I41 by molecular-replacement methods, using the orthorhombic crystal structure as a search model. It was then refined in a unit cell of dimensions a = b = 203.6 and c = 144.6,Å, yielding R and Rfree of 0.196 and 0.244, respectively, for all data at 2.4,Å resolution. A major difference of the HEC structure in the tetragonal crystal compared with the orthorhombic structure was the omission of a 20-residue N-terminal segment corresponding to the first exon of the human catalase gene. The overall structures were otherwise identical in both crystal forms. The NADPH-binding sites were empty in all four subunits and bound water molecules were observed at the active sites. The structure of the C-terminal segment, which corresponds to the last exon, remained undetermined. The tetragonal crystals showed a pseudo-4122 symmetry in molecular packing. Two similar types of lattice contact interfaces between the HEC tetramers were observed; they were related by the pseudo-dyad axes. [source] Crystallization and preliminary crystallographic analysis of bifunctional ,-glutamylcysteine synthetase,glutatione synthetase from Streptococcus agalactiaeACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2009Yasunori Nakashima ,-Glutamylcysteine synthetase,glutathione synthetase (,GCS-GS) is a bifunctional enzyme that catalyzes two consecutive steps of ATP-dependent peptide formation in glutathione biosynthesis. Streptococcus agalactiae,GCS-GS is a target for the development of potential therapeutic agents. ,GCS-GS was crystallized using the sitting-drop vapour-diffusion method. The crystals grew to dimensions of 0.3 × 0.2 × 0.2,mm under reducing conditions with 5,mM TCEP. X-ray data were collected to 2.8,Å resolution from a tetragonal crystal that belonged to space group I41. [source] Surface free energies of isotactic polybutene-1 tetragonal and trigonal crystals: the role of conformational entropy of side chainsJOURNAL OF APPLIED CRYSTALLOGRAPHY, Issue 2007Motoi Yamashita Lateral and end surface free energies of melt-crystallized isotactic polybutene-1 (it-PB1) trigonal and tetragonal crystals have been determined by small-angle X-ray scattering and in situ observation of the crystal growth kinetics. The lateral surface free energy , of the trigonal phase is about seven times as large as the value ,Hoff calculated according to Hoffman's equation [Hoffman (1992). Polymer, 33, 2643,2644], while that of the tetragonal phase is roughly in agreement with the estimation. The discrepancy between the values of , and ,Hoff for the trigonal phase can be attributed to the loss of conformational entropy of the ethyl side chains of it-PB1. [source] Determination of all misorientations of tetragonal lattices with low multiplicity; connection with Mallard's rule of twinningACTA CRYSTALLOGRAPHICA SECTION A, Issue 4 2003Hans Grimmer Two congruent lattices are considered, which are misoriented in such a way that they have a fraction 1, of symmetry translations in common. Whereas for cubic lattices body or face centring does not affect the `multiplicity' or `twin index' ,, this is not generally true for tetragonal lattices. Consider a fixed misorientation and let ,P and ,I be the multiplicities for tP and tI lattices with the same axial ratio ca. Grimmer [Mater. Sci. Forum (1993), 126,128, 269,272] has given an explicit formula for ,P (depending on the misorientation and the axial ratio) and showed that ,I = ,P2, ,P or 2,P. Here stronger results on the occurrence of the three possibilities are presented. Lists of all axial ratios ca of tP and tI lattices admitting misorientations with ,, 5 are given. For each of these misorientations, the twin mirror planes and their normals are listed, so that a synopsis of all possible twin laws of tetragonal crystals by reticular merohedry with ,, 5 is obtained. It is shown that the two twin laws observed in ,-Sn can be described by reticular pseudomerohedry with ,I,=,2 and obliquity ,,=,2.6134°. [source] Structure of the C-terminal domain of nsp4 from feline coronavirusACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2009Ioannis Manolaridis Coronaviruses are a family of positive-stranded RNA viruses that includes important pathogens of humans and other animals. The large coronavirus genome (26,31,kb) encodes 15,16 nonstructural proteins (nsps) that are derived from two replicase polyproteins by autoproteolytic processing. The nsps assemble into the viral replication,transcription complex and nsp3, nsp4 and nsp6 are believed to anchor this enzyme complex to modified intracellular membranes. The largest part of the coronavirus nsp4 subunit is hydrophobic and is predicted to be embedded in the membranes. In this report, a conserved C-terminal domain (,100 amino-acid residues) has been delineated that is predicted to face the cytoplasm and has been isolated as a soluble domain using library-based construct screening. A prototypical crystal structure at 2.8,Å resolution was obtained using nsp4 from feline coronavirus. Unmodified and SeMet-substituted proteins were crystallized under similar conditions, resulting in tetragonal crystals that belonged to space group P43. The phase problem was initially solved by single isomorphous replacement with anomalous scattering (SIRAS), followed by molecular replacement using a SIRAS-derived composite model. The structure consists of a single domain with a predominantly ,-helical content displaying a unique fold that could be engaged in protein,protein interactions. [source] Intermonomer interactions in dimer of bovine heart cytochrome c oxidaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2001Soo Jae Lee The X-ray structure of bovine heart cytochrome c oxidase solved for orthorhombic crystals showed a dimeric structure stabilized by four subunit,subunit contacts, namely, subunit Vb,subunit Vb on the matrix side, subunit I,subunit VIa, subunit VIa,subunit I in the transmembrane region and subunit VIb,subunit VIb on the intermembrane side. The same intermonomer contacts as in the orthorhombic crystals were observed in both hexagonal and tetragonal crystals, the X-ray structures of which were determined by the molecular-replacement method. These results suggest that the dimeric structure also exists under physiological conditions. These contacts, especially the subunit IVa,subunit I contact, in which the N-terminal portion of subunit IVa is placed on the surface of subunit I near the dioxygen-reduction site, indicate that the function of the bovine heart enzyme is likely to be controlled by perturbation of the monomer,monomer association. [source] Structure of tetragonal crystals of human erythrocyte catalaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2001Martin K. Safo The structure of catalase from human erythrocytes (HEC) was determined in tetragonal crystals of space group I41 by molecular-replacement methods, using the orthorhombic crystal structure as a search model. It was then refined in a unit cell of dimensions a = b = 203.6 and c = 144.6,Å, yielding R and Rfree of 0.196 and 0.244, respectively, for all data at 2.4,Å resolution. A major difference of the HEC structure in the tetragonal crystal compared with the orthorhombic structure was the omission of a 20-residue N-terminal segment corresponding to the first exon of the human catalase gene. The overall structures were otherwise identical in both crystal forms. The NADPH-binding sites were empty in all four subunits and bound water molecules were observed at the active sites. The structure of the C-terminal segment, which corresponds to the last exon, remained undetermined. The tetragonal crystals showed a pseudo-4122 symmetry in molecular packing. Two similar types of lattice contact interfaces between the HEC tetramers were observed; they were related by the pseudo-dyad axes. [source] Crystallization and preliminary X-ray diffraction data of mouse L-chain apoferritin crystalsACTA CRYSTALLOGRAPHICA SECTION D, Issue 5 2000Thierry Granier Crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique using ammonium sulfate as precipitant. Two crystal forms were observed in the same drop. The crystals belong to either the P2 monoclinic or to the P4212 tetragonal space group. The monoclinic crystals diffracted to beyond 2.4,Å resolution but were systematically twinned, while the tetragonal crystals diffracted to beyond 2.9,Å. These crystallization conditions in the absence of metal salts should facilitate the study of the interaction between L-chain ferritins and heavy metals, particularly the iron core. [source] Preliminary crystallographic analysis of the N-terminal domain of FILIA, a protein essential for embryogenesisACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2010Juke Wang FILIA is a component of the subcortical maternal complex that is essential for early stage embryogenesis. Its 6×His-tagged N-terminal domain was expressed in Escherichia coli and purified to homogeneity. Two types of crystals formed under different crystallization conditions during screening. Orthorhombic crystals appeared in a solution containing 1.4,M ammonium sulfate, 0.1,M Tris pH 8.2 and 12% glycerol, while tetragonal crystals were obtained using 15% PEG 4000 mixed with 0.1,M HEPES pH 7.5 and 15% 2-propanol. High-quality diffraction data were collected from the two crystal forms to resolutions of 1.8 and 2.2,Å, respectively, using synchrotron radiation. The Matthews coefficients indicated that the P212121 and P41212 crystals contained two molecules and one molecule per asymmetric unit, respectively. A selenomethionine-substituted sample failed to crystallize under the native conditions, but another orthorhombic crystal form was obtained under different conditions and anomalous diffraction data were collected. [source] Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniaeACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2010Noella Silva-Martin As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl-7 cleaves the glycosidic ,1,4 bonds between N -acetylmuramic acid and N -acetylglucosamine in the pneumococcal cell wall, resulting in bacterial lysis. Recombinant Cpl-7 was overexpressed in Escherichia coli, purified and crystallized using the vapour-diffusion method at 291,K. Diffraction-quality tetragonal crystals of the catalytic module of Cpl-7 were obtained from a mixture of PEG 3350 and sodium formate. The crystals belonged to space group I422, with unit-cell parameters a = 127.93, b = 127.93, c = 82.07,Å. Diffraction data sets were collected to 2.4,Å resolution using a rotating-anode generator. [source] Structure of the T109S mutant of Escherichia coli dihydroorotase complexed with the inhibitor 5-fluoroorotate: catalytic activity is reflected by the crystal formACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2007Mihwa Lee Crystals of a single-point mutant (T109S) of Escherichia coli dihydroorotase (DHOase) with diminished activity grown in the presence of l -dihydroorotate (l -DHO) are tetragonal, with a monomer in the asymmetric unit. These crystals are extremely unstable and disintegrate shortly after formation, which is followed by the growth of orthorhombic crystals from the remnants of the tetragonal crystals or at new nucleation sites. Orthorhombic crystals, for which a structure has previously been reported [Thoden et al. (2001), Biochemistry, 40, 6989,6997; Lee et al. (2005), J. Mol. Biol.348, 523,533], contain a dimer of DHOase in the asymmetric unit; the active site of one monomer contains the substrate N -carbamyl- l -aspartate (l -CA-asp) and the active site of the other monomer contains the product of the reaction, l -DHO. In the subunit with l -DHO in the active site, a surface loop (residues 105,115) is `open'. In the other subunit, with l -CA-asp in the active site, the loop folds inwards, forming specific hydrogen bonds from the loop to the l -CA-asp. The tetragonal crystal form can be stabilized by crystallization in the presence of the inhibitor 5-fluoroorotate (FOA), a product (l -DHO) mimic. Crystals of the complex of T109S DHOase with FOA are tetragonal, space group P41212, with unit-cell parameters a = b = 72.6, c = 176.1,Å. The structure has been refined to R and Rfree values of 0.218 and 0.257, despite severe anisotropy of the diffraction. In this structure, the flexible loops are both in the `open' conformation, which is consistent with FOA, like l -DHO, binding at both sites. The behaviour of the T109S mutant crystals of DHOase in the presence of l -DHO is explained by initial binding of l -DHO to both subunits, followed by slow conversion to l -CA-asp, with consequent movement of the flexible loop and dissolution of the crystals. Orthorhombic crystals are then able to grow in the presence of l -DHO and l -CA-asp. [source] | ||||||||||