Powder X-ray characterization of lithium thiazoildine-4-carboxylate

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

X-ray powder diffraction analysis of a new palladium(II) amino acid complex

Powder X-ray diffraction data for a new palladium(II) amino acid complex, of composition PdC12H2ON2O4S2, are presented in this paper. Orthorhombic cell parameters are: a = 10.740 angstrom, b = 19.999 angstrom, and c = 5.2470 angstrom. (c) 2004 International Centre for Diffraction Data.

X-ray powder diffraction analysis of methionine sulfoxide

Powder X-ray diffraction data for methionine sulfoxide, C5H11NO3S, obtained from the commercial amino acid, are presented in this work. Monoclinic cell parameters are: a = 15.500 Angstrom; b = 3.820 Angstrom; c = 13.490 Angstrom; 8=97.300 degrees. (C) 2001 International Centre for Diffraction Data.

X-ray diffraction and mossbauer spectra of nickel ferrite prepared by combustion reaction

Nickel ferrite powders with a nominal NiFe2O4 composition were synthesized by combustion reaction using urea as fuel. The powder was obtained using a vitreous silica basin heated directly on a hot plate at 480 degrees C until self-ignition occurred. After combustion, the powder was calcined at 700 degrees C for 2 h. The formation of the spinel phase and the distribution of cations in the tetrahedral and octahedral sites of the crystal structure were investigated by the Rietveld method, using synchrotron X-ray diffraction data and Mossbauer spectroscopy. The material presented a crystallite size of 120 nm and magnetic properties. The resulting stoichiometry after the Rietveld refinement was (Fe-0.989(2) Ni-0.011(2)) [Fe-1.012(2) Ni-0.989(2)] O-4.

X-ray diffraction data of tibolone Delta(4) isomer (isotibolone)

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

Influence of annealing on X-ray diffraction of natural alexandrite

In this work we present results of X-ray diffraction using powder method, on natural alexandrite samples from Minas Gerais State (Brazil), as a function of a sequence of annealing. From these measurements we determine lattice parameters before (a = 9.405 Angstrom, b = 5.471 Angstrom, c = 4.409 Angstrom) and after annealing, and its structure is confirmed as orthorhombic. Measurements done after an annealing of 15 minutes at 700 degreesC and for 5 hours at 1000 degreesC indicate the migration of atoms present in the sample through different phases, which were also identified by Microprobe Analysis (WDS). However we have verified that such migration does not modify the structure. X-ray diffraction measurements have been carried out in conjunction with optical absorption in the UV-Vis as a function of annealing. (C) 2002 International Centre for Diffraction Data.

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.

Powder X-ray characterization of djenkolic acid

X-ray powder diffraction data for the orthorhombic natural amino acid djenkolic acid, C7H14N2O4S2, is described in this paper. The orthorhombic cell parameters are: a = 8.12 Angstrom, b = 12.16 Angstrom, and c = 5.38 Angstrom . (C) 2001 International Centre for Diffraction Data.

Resonant x-ray diffraction as a tool to calculate mixed valence ratios: Application to Prussian Blue materials

An approach is proposed here to calculate mixed valence ratios in molecular compounds. Synchrotron x-ray powder diffraction experiments were conducted to determine the Fe(+3)/Fe(+2) ratio in Prussian Blue compounds, which were elected as an example of the use of this approach. As a result, a resonant x-ray diffraction measurement provided direct evidence that the vacant [Fe(CN)(6)] group was randomly absent from similar to 31% of the structure, which was indicated by structural differences caused by variations in the anomalous dispersion term. These findings are very important for a deeper understanding of the changes occurring in properties during in situ compositional variations. (c) 2008 American Institute of Physics.

Crystallization and preliminary X-ray diffraction analysis of a eumenine mastoparan toxin: a new class of mast-cell degranulating peptide in the wasp venom

Mastoparans are tetradecapeptides found to be the major component of vespid venoms. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized and X-ray diffraction data collected to 2.7 Angstrom resolution using a synchrotron-radiation source. Crystals were determined to belong to the space group P6(2)22 (P6(4)22). This is the first mastoparan to be crystallized and will provide further insights into the conformational significance of mastoparan toxins with respect to their potency and activity in G-protein regulation.

Crystallization and preliminary X-ray diffraction analysis of a glutathione S-transferase from Xylella fastidiosa

Glutathione S-transferases (GSTs) form a group of multifunctional isoenzymes that catalyze the glutathione-dependent conjugation and reduction reactions involved in the cellular detoxification of xenobiotic and endobiotic compounds. GST from Xylella fastidiosa (xfGST) was overexpressed in Escherichia coli and purified by conventional affinity chromatography. In this study, the crystallization and preliminary X-ray analysis of xfGST is described. The purified protein was crystallized by the vapour-diffusion method, producing crystals that belonged to the triclinic space group P1. The unit-cell parameters were a = 47.73, b = 87.73, c = 90.74 angstrom, alpha = 63.45, beta = 80.66, gamma = 94.55 degrees. xfGST crystals diffracted to 2.23 angstrom resolution on a rotating-anode X-ray source.

Crystallization and preliminary X-ray diffraction analysis of importin-alpha acomplexed with NLS peptidomimetics

Importin-alpha is the nuclear import receptor that recognizes cargo proteins with nuclear localization sequences (NLSs). Tile study of NLS peptidomimetics can provide a better understanding of the requirements for the molecular recognition of cargo proteins by importin-alpha, and potentially engender a large number of applications in medicine. Importin-a was crystallized with a set of six NLS peptidomimetics, and X-ray diffraction data were collected in the range 2.1-2.5 angstrom resolution. Preliminary electron density calculations show that the ligands are present in the crystals. (c) 2005 Elsevier B.V All rights reserved.

Crystallization and preliminary X-ray diffraction analysis of a myotoxic phospholipase A(2) homologue from Bothrops neuwiedi pauloensis venom

Crystals of a myotoxic phospholipase A(2) from Bothrops neuwiedi pauloensis have been obtained. They diffracted at 2.5 Angstrom resolution using a synchrotron radiation source and belong to space group P3(1)21. Preliminary analysis shows that there are two molecules in the asymmetric unit. (C) 1999 Elsevier B.V. B.V. All rights reserved.

Crystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A(2) complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors at 1.9-and 1.45-A resolution

An acidic phospholipase A(2) (PLA(2)) isolated from Bothrops jararacussu snake venom was crystallized with two inhibitors: alpha-tocopherol (vitamin E) and p-bromophenacyl bromide (BPB). The crystals diffracted at 1.45- and 1.85-Angstrom resolution, respectively, for the complexes with alpha-tocopherol and p-bromophenacyl bromide. The crystals are not isomorphous with those of the native protein, suggesting the inhibitors binding was successful and changes in the quaternary structure may have occurred. (C) 2004 Elsevier B.V. All rights reserved.

Crystallization and preliminary X-ray diffraction analysis of a myotoxic Lys49-PLA(2) from Bothrops jararacussu venom complexed with p-bromophenacyl bromide

For the first time, a non-catalytic and myotoxic Lys49-PLA(2) (BthTX-I from Bothrops jararacussu venom) has been crystallized with BPB inhibitor. X-ray diffraction data were collected and electron-density calculations showed that the ligand is bound to the His48 residue. BthTX-I with His48 chemically modified by BPB shows strongly reduced myotoxic and cytotoxic activities. This suggests a biological correlation between the modification of His48, which is associated with catalytic activity of PLA(2)s, and other toxicological activities of Lys49-PLA(2)s.