Purification, crystallization and preliminary X-ray diffraction analysis of carboxyhaemoglobin-II from the fish Piaractus mesopotamicus (pacu)

Carboxyhaemoglobin-II isolated from the pacu (Piaractus mesopotamicus) has been crystallized and X-ray diffraction data were collected to 2.0 Angstrom resolution using synchrotron radiation. Crystals were characterized as belonging to the space group I23; preliminary structural analysis reveals the presence of one dimer in the asymmetric unit.

Crystallization and preliminary X-ray diffraction analysis of prephenate dehydratase from Mycobacterium tuberculosis H37Rv

Tuberculosis remains the leading cause of mortality arising from a bacterial pathogen ( Mycobacterium tuberculosis). There is an urgent need for the development of new antimycobacterial agents. The aromatic amino-acid pathway is essential for the survival of this pathogen and represents a target for structure-based drug design. Accordingly, the M. tuberculosis prephenate dehydratase has been cloned, expressed, purified and crystallized by the hanging-drop vapour-diffusion method using PEG 400 as a precipitant. The crystal belongs to the orthorhombic space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 98.26, b = 133.22, c = 225.01 angstrom, and contains four molecules in the asymmetric unit. A complete data set was collected to 3.2 angstrom resolution using a synchrotron-radiation source.

Crystallization and preliminary X-ray diffraction analysis of XAC1151, a small heat-shock protein from Xanthomonas axonopodis pv. citri belonging to the alpha-crystallin family

The hspA gene (XAC1151) from Xanthomonas axonopodis pv. citri encodes a protein of 158 amino acids that belongs to the small heat-shock protein ( sHSP) family of proteins. These proteins function as molecular chaperones by preventing protein aggregation. The protein was crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium phosphate. X-ray diffraction data were collected to 1.65 angstrom resolution using a synchrotron-radiation source. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 128.7, c = 55.3 angstrom. The crystal structure was solved by molecular-replacement methods. Structure refinement is in progress.

Crystal structure and infrared analysis of a new trinuclear platinum(II) complex with L-cysteine

A new trinuclear platinum(II) complex with cysteine of composition [Pt(C3H6NO2S)Cl](3)center dot(C2H6SO)(3) was obtained and structurally characterized by X-ray diffraction and infrared analysis. The compound crystallizes in the trigonal system, space group R3, and is described in a hexagonal cell with a=17.739(1), c=9.531(1) and Z=3. Cysteine is coordinated to Pt(II) through the nitrogen and sulphur atoms. Each cysteine sulphur bridges between two metal atoms. A square planar coordination sphere of platinum is completed by a chlorine atom. The complex is soluble in dimethyl sulfoxide.

Purification, crystallization and Patterson search of haemoglobin IV from the armoured catfish Liposarcus anisitsi

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Structure of human uropepsin at 2.45 angstrom resolution

The molecular structure of human uropepsin, an aspartic proteinase from the urine produced in the form of pepsinogen A in the gastric mucosa, has been determined by molecular replacement using human pepsin as the search model. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.99, b = 75.56, c = 89.90 Angstrom. Crystallographic refinement led to an R factor of 0.161 at 2.45 Angstrom resolution. The positions of 2437 non-H protein atoms in 326 residues have been determined and the model contains 143 water molecules. The structure is bilobal, consisting of two predominantly beta -sheet lobes which, as observed in other aspartic proteinases, are related by a pseudo-twofold axis. A model of the uropepsin-pepstatin complex has been constructed based on the high-resolution crystal structure of pepsin complexed with pepstatin.

Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: New insights into the understanding of the structure-biological activity relationship in legume lectins

Plant lectins, especially those purified from species of the Legummosae family, represent the best studied group of carbohydrate-binding proteins. The legume lectins from Diocleinae subtribe are highly similar proteins that present significant differences in the potency/ efficacy of their biological activities. The structural studies of the interactions between lectins and sugars may clarify the origin of the distinct biological activities observed in this high similar class of proteins. In this way, this work presents a crystallographic study of the ConM and CGL (agglutinins from Canavalia maritima and Canavalia gladiata, respectively) in the following complexes: ConM/ CGL:Man(alpha 1-2)Man(alpha 1-0)Me, ConM/CGL:Man(alpha 1-O)Man(alpha 1-O)Me and ConM/CGL:Man(alpha 1-4)Man(alpha 1-O)Me, which crystallized in different conditions and space group from the native proteins.The structures were solved by molecular replacement, presenting satisfactory values for R-factor and R-factor. Comparisons between ConM, CGL and ConA (Canavalia ensiformis lectin) binding mode with the dimannosides in subject, presented different interactions patterns, which may account for a structural explanation of the distincts biological properties observed in the lectins of Diocleinae subtribe. (C) 2007 Elsevier B.V. All rights reserved.

Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A(2) homologue from Zhaoermia mangshanensis venom

Zhaoermiatoxin, an Arg49 phospholipase A(2) homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis, Ermia mangshanensis) venom is a novel member of the PLA(2)-homologue family that possesses an arginine residue at position 49, probably arising from a secondary Lys49 -> Arg substitution that does not alter the catalytic inactivity towards phospholipids. Like other Lys49 PLA(2) homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA(2) catalytic activity. A single crystal with maximum dimensions of 0.2 x 0.2 x 0.5 mm was used for X-ray diffraction data collection to a resolution of 2.05 angstrom using synchrotron radiation and the diffraction pattern was indexed in the hexagonal space group P6(4), with unit-cell parameters a = 72.9, b = 72.9, c = 93.9 angstrom.

Crystal structures and luminescence properties of La3Zr4F25 and alpha-LaZr3F15

During a study of the LaF3-ZrF4 system, both La3Zr4F25 and alpha-LaZr3F15 compounds have been evidenced. Their crystal structures have been determined from single-crystal X-ray diffraction data. La3Zr4F25 crystallises in the cubic system with a= 12.384 Angstrom and I (4) over bar 3d space group (no. 220). Its crystal structure is built up of (ZrF6)(2-) octahedra and (LaF8)(5-) dodecahedra sharing corners. The low temperature form, alpha, of LaZr3F15 is orthorhombic (space group Pmmn, no. 59) with a = 15.721 Angstrom, b = 16.299 Angstrom, c= 8.438 Angstrom. Its structure is built of corner-sharing tricaped trigonal prisms surrounding the La3+ ions and both octahedra and monocapped trigonal prisms encompassing the Zr4+ ions. This structure is characterised by dynamically disordered (ZrF6)(2-) complex anions.The Eu3+ luminescence properties of these phases have been investigated and are discussed in relationship with their crystal structures.

Synthesis, structure and redox properties of an unexpected trinuclear copper(II) complex with aspartame: [Cu(apm)(2)Cu(mu-N,O : O '-apm)(2)(H2O)Cu(apm)(2)(H2O)]center dot 5H(2)O

Structural, magnetic and spectroscopic data of a new trinuclear copper(II) complex with the ligand aspartame (apm) are described. [Cu(apm)(2)CU(mu-N,O:O'-apm)(2)(H2O)Cu(apm)(2)(H2O)]-5H(2)O crystallizes in the triclinic system, space group P1 (#1) with a = 7.3300(1) angstrom, b = 15.6840(1) angstrom, c = 21.5280(1) angstrom, alpha = 93.02(1)degrees, beta = 93.21 (1)degrees, gamma = 92.66(1)degrees and Z = 1. Aspartame coordinates to Cu(II) through the carboxylate and beta-amino groups. The carboxylate groups of the two central ligands act as bidentate bridges in a syn-anti conformation while the carboxylate groups of the four peripheral ligands are monodentate in a syn conformation. The central copper ion is in a distorted square pyramidal geometry with the apical position being occupied by one oxygen atom of the water molecule. The two terminal copper(II) atoms are coordinated to the ligands in the same position but their coordination sphere differs from each other due to the fact that one copper atom has a water molecule in an apical position leading to an octahedral coordination sphere while the other copper atom is exclusively coordinated to aspartame ligands forming a distorted square pyramidal coordination sphere. Thermal analysis is consistent with the X-ray structure. EPR spectra and CV curves indicate a rupture of the trinuclear framework when this complex is dissolved in ethanol or DMF, forming a mononuclear species, with a tetragonal structure. (c) 2005 Elsevier B.V. All rights reserved.

X-ray powder data and bond valence of La0.65Sr0.35MnO3 after Rietveld refinement

Powder X-ray diffraction (XRD) data were collected for La0.65Sr0.35MnO3 prepared through an alternative method from a stoichiometric mixture of Mn2O3, La2O3, and SrO2, fired at 1300 degreesC for 16 h. XRD analysis using the Rietveld method was carried out and it was found that manganite has rhombohedral symmetry (space group R(3) over bar c). The lattice parameters are found to be a=5.5032 Angstrom and c=13.3674 Angstrom. The bond valence computation indicates that the initial inclusion of Sr occurs at higher temperature. (C) 2002 International Centre for Diffraction Data.

Crystallization and preliminary X-ray diffraction analysis of an anti-H(O) lectin from Lotus tetragonolobus seeds

The seed lectin from Lotus tetragonolobus (LTA) has been crystallized. The best crystals grew over several days and were obtained using the vapour-diffusion method at a constant temperature of 293 K. A complete structural data set was collected at 2.00 angstrom resolution using a synchrotron-radiation source. LTA crystals were found to be monoclinic, belonging to space group P2(1), with unit-cell parameters a = 68.89, b = 65.83, c = 102.53 angstrom, alpha = gamma = 90, beta = 92 degrees. Molecular replacement yielded a solution with a correlation coefficient and R factor of 34.4 and 51.6%, respectively. Preliminary analysis of the molecular-replacement solution indicates a new quaternary association in the LTA structure. Crystallographic refinement is under way.

Crystallization of piratoxin I, a myotoxic LYS49-phospholipase A(2) homologue isolated from the venom of Bothrops pirajai

Fernanda Canduri, Lit C. Mancuso, Andreimar M. Soares, Jose R. Giglio, Richard J. Ward and Raghuvir K. Arni. Crystallization of piratoxin I, a myotoxic Lys49-phospholipase A(2) homologue isolated from the venom of Bothrops pirajai. Toxicon 36, 547-551, 1998.-Large single crystals of piratoxin I, a Lys49-PLA(2) homologue with low enzymatic activity, have been obtained. The crystals belong to the orthorhombic system space group p2(1)2(1)2(1) and diffract X-raps to a resolution of 2.8 Angstrom. Preliminary analysis reveals the presence of two molecules in the crystallographic asymmetric unit. (C) 1998 Elsevier B.V. Ltd. All rights reserved.

Crystallization and preliminary X-ray diffraction analysis of suramin, a highly charged polysulfonated napthylurea, complexed with a myotoxic PLA(2) from Bothrops asper venom

Suramin is a highly charged polysulfonated napthylurea that interferes in a number of physiologically relevant processes such as myotoxicity, blood coagulation and several kinds of cancers. This synthetic compound was complexed with a myotoxic Lys49 PLA(2) from Bothrops asper venom and crystallized by the hanging-drop vapor diffusion method at 18 degreesC. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters a=49.05, b=63.84 and c=85.67 Angstrom, Diffraction data was collected to 1.78 Angstrom. (C) 2004 Elsevier B.V. All rights reserved.

X-ray powder diffraction analysis of a silver(I)-aspartame complex

Synchrotron X-ray powder diffraction (XRPD) data were collected for the silver(I)-aspartame complex [Ag(C14H17N2O5)]center dot 1/2 H2O. The complex was obtained from a stoichiometric mixture of aspartame (3-amino-N-(alpha-carboxyphenethyl)-succinamic acid N-methyl ester, C14H18N2O5), Na2CO3, and AgNO3. Indexing using Crysfire and Chekcell proposed an orthorhombic unit cell with space group P222(1). The lattice parameters are a = 12.4750(1) angstrom, b = 21.60614(14) angstrom, and c = 4.88888(9) angstrom. (C) 2006 International Centre for Diffraction Data.