RESUMO
Because of their high electrical conductivity CoSi2 nanostructures are potential candidates for preparing ordered nano-arrays to be used as electrode interconnectors and contacts in microelectronic devices. We here describe a controlled procedure for the endotaxial growth of hexagonal CoSi2 nanoplatelets buried in differently oriented single crystalline Si wafers on which a Co-doped SiO2 thin film was previously deposited. These nanomaterials were obtained by a clean procedure consisting of isothermal annealing at 750 °C under a He atmosphere of Co-doped SiO2 thin films deposited onto the surface of three differently oriented flat Si substrates, namely Si(001), Si(011) and Si(111). Buried CoSi2 nanoplatelets are in all cases spontaneously formed as a consequence of the diffusion of Co atoms into the silicon wafer and their reaction with host Si atoms. Our TEM and GISAXS analyses demonstrated that these arrays, irrespective of host Si orientation, consist of CoSi2 hexagonal nanoplatelets in all cases parallel to Si{111} crystallographic planes. Additionally, the dimensions of the nanoplatelets were consistently determined by TEM and GISAXS for the three different host Si single crystal orientations.
RESUMO
The purpose of the designed reactor is (i) to obtain polycrystalline and∕or amorphous thin films by controlled deposition induced by a reactive sputtering magnetron and (ii) to perform a parallel in situ structural study of the deposited thin films by X-ray diffraction, in real time, during the whole growth process. The designed reactor allows for the control and precise variation of the relevant processing parameters, namely, magnetron target-to-sample distance, dc magnetron voltage, and nature of the gas mixture, gas pressure and temperature of the substrate. On the other hand, the chamber can be used in different X-ray diffraction scanning modes, namely, θ-2θ scanning, fixed α-2θ scanning, and also low angle techniques such as grazing incidence small angle X-ray scattering and X-ray reflectivity. The chamber was mounted on a standard four-circle diffractometer located in a synchrotron beam line and first used for a preliminary X-ray diffraction analysis of AlN thin films during their growth on the surface of a (100) silicon wafer.
RESUMO
A nanocomposite consisting of PbTe nanocrystals embedded in a silicate glass was studied by small-angle x-ray scattering during the early stage of isothermal annealing at 793 K. A theoretical function based on a model of spherical PbTe nanocrystals surrounded by a Pb and Te depleted shell fits well to all experimental curves. The time dependences of the nanocrystal radius and size of the depleted shell agree with the prediction of the theory of nucleation and growth by the classical mechanism of atomic diffusion.
RESUMO
ATP-dependent phosphoenolpyruvate carboxykinase (PEPCK) (ATP: oxaloacetate carboxylyase (transphosphorylating), EC 4.1.1.49) is a key enzyme involved in the catabolism of glucose and amino acids in the parasite Trypanosoma cruzi, the causative agent of Chagas' disease. Due to the significant differences in the amino acid sequence and substrate specificity of the human enzyme (PEPCK (GTP-dependent), EC 4.1.1.32), the parasite enzyme has been considered a good target for the development of new anti-chagasic drugs. We have solved the crystal structure of the recombinant PEPCK of T. cruzi up to 2.0 A resolution, characterised the dimeric organisation of the enzyme by solution small angle X-ray scattering (SAXS) and compared the enzyme structure with the known crystal structure of the monomeric PEPCK from Escherichia coli. The dimeric structure possesses 2-fold symmetry, with each monomer sharing a high degree of structural similarity with the monomeric structure of the E. coli PEPCK. Each monomer folds into two complex mixed alpha/beta domains, with the active site located in a deep cleft between the domains. The two active sites in the dimer are far apart from each other, in an arrangement that seems to permit an independent access of the substrates to the two active sites. All residues of the E. coli PEPCK structure that had been found to interact with substrates and metal cofactors have been found conserved and in a substantially equivalent spatial disposition in the T. cruzi PEPCK structure. No substrate or metal ion was present in the crystal structure. A sulphate ion from the crystallisation medium has been found bound to the active site. Solution SAXS data suggest that, in solutions with lower sulphate concentration than that used for the crystallisation experiments, the actual enzyme conformation may be slightly different from its conformation in the crystal structure. This could be due to a conformational transition upon sulphate binding, similar to the ATP-induced transition observed in the E. coli PEPCK, or to crystal packing effects. The present structure of the T. cruzi PEPCK will provide a good basis for the modelling of new anti-chagasic drug leads.
Assuntos
Fosfoenolpiruvato Carboxiquinase (ATP)/química , Trypanosoma cruzi/enzimologia , Sequência de Aminoácidos , Animais , Sítios de Ligação , Doença de Chagas/tratamento farmacológico , Coenzimas/metabolismo , Sequência Conservada , Cristalização , Dimerização , Desenho de Fármacos , Escherichia coli/enzimologia , Modelos Moleculares , Dados de Sequência Molecular , Fosfoenolpiruvato Carboxiquinase (ATP)/antagonistas & inibidores , Estrutura Quaternária de Proteína , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Alinhamento de Sequência , Sulfatos/metabolismo , Difração de Raios XRESUMO
The synchrotron light source designed and constructed at the LNLS is composed of a 1.37 GeV electron storage ring and a 120 MeV linac for low-energy injection. The storage ring has been commissioned and has already reached the designed electron-beam energy, current and emittance. The electron lifetime is now 6 h at 60 mA, and is steadily increasing. Seven beamlines (TGM, SGM, SXS, XAFS, XRD, SAXS, PCr) have been constructed in parallel with the electron accelerators and are at present in operation. Beam time was allocated to 129 approved research projects for the second semester of 1997. A number of them are currently under way.
RESUMO
Small-angle X-ray scattering (SAXS) was used to study structural characteristics of human serum albumin (HSA) in solution under different pH conditions. Guinier analysis of SAXS results yielded values of the molecular radius of gyration ranging from 26.7 A to 34.5 A for pH varying from 2.5 to 7.0. This suggests the existence of significant differences in the overall shape of the molecule at different pH. Molecular models based on subdomains with different spatial configurations were proposed. The distance distribution functions associated with these models were calculated and compared with those determined from the experimental SAXS intensity functions. The conclusion of this SAXS study is that the arrangement of molecular subdomains is clearly pH dependent; the molecule adopting more or less compact configuration for different pH conditions. The conclusions of this systematic study on the modification in molecular shape of HSA as a response to pH changes is consistent with those of previous investigations performed for particular pH conditions.
Assuntos
Albumina Sérica/química , Fenômenos Químicos , Físico-Química , Humanos , Concentração de Íons de Hidrogênio , Conformação Proteica , Espalhamento de Radiação , Soluções , Raios XRESUMO
The structure of crotapotin, a protein extracted, from the venom of the Crotalus durissus terrificus, in solution at pH = 1.5, was studied by SAXS. The experimental results yield structural parameter values of the molecular radius of gyration Rg = 13.6 A, volume v = 16.2 x 10(3) A3 A3 and maximal dimension Dmax = 46 A. The distance distribution function deduced from the scattering measurements is consistent with an overall molecular shape of an oblate ellipsoid of revolution with asymmetry parameter v = 0.45.
Assuntos
Crotoxina/química , Animais , Fenômenos Biofísicos , Biofísica , Concentração de Íons de Hidrogênio , Espalhamento de Radiação , Soluções , Raios XRESUMO
alpha-crotamine is a small toxic protein (42 amino acid residues with three disulphide bridges) present in the venom of Crotallus durissus terrificus. Molecular parameters (Rg = 13.7 A, S = 3,000 A2, V = 9,200 A3 and Dmax = 40 A) were derived from SAXS curves obtained from a solution of this protein at pH = 4.5. An excellent agreement between the experimental distance distribution curve and that calculated from a model consisting of two lobes linked by the Cys(18)-Cys(30) disulphide bridge.