Avrami exponent of crystallization in tellurite glasses

Nucleation process and crystal growth for three samples of the (20-x)Li(2)O-80TeO(2)-xWO(3) glass system were studied using X-ray diffraction and differential scanning calorimetry techniques. X-ray diffraction data confirmed the amorphous characteristic of the as-quenched samples and indicated the growth of crystalline phases formed due to the thermal treatment for annealed samples. These results reveal the presence of three distinct gamma-TeO(2), alpha-TeO(2) and alpha-Li(2)Te(2)O(5) crystalline phases in the TL sample, and two distinct alpha-TeO(2) and gamma-TeO(2) crystalline phases in the TLW5 and TLW10 samples. The activation energy and the Avrami exponent were determined from DSC measurements. The activation energy values X-ray diffraction data of the TLW10 glass sample suggest that gamma-TeO(2) phase occur before the alpha-TeO(2). The results obtained for the Avrami exponent point to that the nucleation process is volumetric and that the crystal growth is two or three-dimensional.

Effects of glass-forming histories on the crystallization kinetic of the 20Li(2)O-80TeO(2) glass

In the present work, tellurite 20Li(2)O-80TeO(2) glasses were prepared with identical nominal composition under different glass-forming histories to produce a stressed and stress-free samples. X-ray Diffraction (XRD) and Differential Scanning Calorimetry (DSC) techniques were used to study the effects of the glass-forming histories on the thermal and structural properties of these glasses. The gamma-TeO2 (metastable), alpha-TeO2 and alpha-Li2Te2O5 phases were identified during the controlled devitrification in these glasses. The mestastable character of the gamma-TeO2 phase was clearly observed in the glass under stress but this effect is not so clear in the stress-free glass. The gamma-TeO2 and alpha-TeO2 phases crystallizes during the initial stages of crystallization in both studied glasses while the alpha-Li2Te2O5 phase crystallize in the final stages of the crystallization. The activation energies and Avrami exponent were calculated for both studied glasses with different particle size leading to E-3 > E-2 > E-1 for stressed glass and E-3 > E-2 approximate to E-1 for stress-free glass, where E-1, E-2 and E-3 were associated to the gamma-TeO2, alpha-TeO2 and alpha-Li2Te2O5 phases, respectively. The observed distinct (n) over bar (1) < <(n)over bar>(2) < <(n)over bar>(3) in both glasses is an indicative that nucleation and growth takes place by more than one mechanism in the early stages of the crystallization. (C) 2011 Elsevier B.V. All rights reserved.

Thermally stimulated crystallization glass system of (20-x)LiO2-80TeO(2)-xWO(3)

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Crystallization kinetics and thermal properties of 20Li(2)O-80TeO(2) glass

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

NON-ISOTHERMAL STUDIES on CRYSTALLIZATION KINETICS of TELLURITE 20Li(2)O-80TeO(2) GLASS

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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.

Crystallization and preliminary x-ray analysis of Parkia pendula lectin

Lectins are proteins important in various biological processes such as infection, cell differentiation and metastasis. The Parkia pendula lectin has been crystallized using the hanging-drop vapour diffusion method. X-ray diffraction data were collected using a Rigaku RU300 rotating anode generator and R-AXIS IV diffractometer. The cell parameters for P. pendula lectin are a=93.7 Angstrom b=161.1 Angstrom, c=80.0 Angstrom and space group C222. The maximum resolution was of 2.98 Angstrom. These data showed a R-sym=12.8%.

Crystallization, preliminary X-ray analysis and Patterson search of a new aspartic protease isolated from human urine

Aspartic protease (EC 3.4.23) make up a widely distributed class of enzymes in animals, plants, microbes and, viruses. In animals these enzymes perform diverse functions, which range from digestion of food proteins to very specific regulatory roles. In contrast the information about the well-characterized aspartic proteases, very little is known about the corresponding enzyme in urine. A new aspartic protease isolated from human urine has been crystallized and X-ray diffraction data collected to 2.45 Angstrom resolution using a synchrotron radiation source. Crystals belong to the space group P2(1)2(1)2(1) the cell parameters obtained were a=50.99, b=75.56 and c=89.90 Angstrom. Preliminary analysis revealed the presence of one molecule in the asymmetric unit. The structure was determined using the molecular replacement technique and is currently being refined using simulated annealing and conjugate gradient protocols.

Crystallization and preliminary X-ray analysis of S-III-SPIII, a phospholipase A2 isolated from the venom of Bothrops jararacussu.

Large single crystals have been obtained of S-III-SPIII, a phospholipase A(2) from the venom of Bothrops jararacussu. The crystals belong to the orthorhombic system space group C222, and diffract X-rays to a resolution of 1.9 Angstrom. Preliminary analysis reveals the presence of one molecule in the crystallographic asymmetric unit. The crystal structure is currently being determined using molecular replacement techniques.

Crystallization and preliminary X-ray diffraction studies of two myotoxic Lys49-phospholipases A(2) complexed with alpha-tocopherol

BnSP-7 and BnSP-6, two Lys49-phospholipase A(2) isolated from Bothrops neuwiedi pauloensis snake venom, were co-crystallized with a-tocopherol and X-ray diffraction data were collected for both complexes (2.2 and 2.6 angstrom). A new alternative quaternary conformation for these two complexes compared with all other dimeric Lys49-PLA(2) has been observed.

Crystallization and preliminary X-ray diffraction studies of BnSP-6, a myotoxic phospholipase A2 from Bothrops neuwiedi venom

BnSP-6 (myotoxin I) is a phospholipase A2 homologue isolated from Bothrops neuwiedi pauloensis venom. Crystals of BnSP-6 were obtained which diffracted X-rays to 2.5 Angstrom resolution using a synchrotron radiation source at room temperature and belong to space group P3(1)21. The unit cell dimensions are a=b=57.7, c=131.1 Angstrom. The structure was solved by molecular replacement using the coordinates of bothropstoxin I from B. jararacussu venom. There are two molecules in the asymmetric unit.