Preliminary Crystallographic Data (preliminary + crystallographic_data)

Distribution by Scientific Domains


Selected Abstracts


Preliminary crystallographic data of the three homologues of the thiol,disulfide oxidoreductase DsbA in Neisseria meningitidis.

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2008
Corrigendum
A correction is made to the name one of the authors of Lafaye et al. [Acta Cryst. (2008). F64, 111,114]. [source]


Crystallization and preliminary crystallographic data of a leucotoxin S component from Staphylococcus aureus

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2004
ValÚrie 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-ş600 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,┼, , = 106.4░ and a = b = 94.8, c = 306.2,┼, respectively. A full set of X-ray diffraction data was collected to 2.1,┼ from a single tetragonal crystal of the wild-type protein at 100,K. [source]


Crystallization and preliminary X-ray crystallographic characterization of a public CMV-specific TCR in complex with its cognate antigen

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 11 2009
Jean-Baptiste Reiser
The T-cell response to human cytomegalovirus is characterized by a dramatic reduction of clonal diversity in patients undergoing chronic inflammation or immunodepression. In order to check whether all the selected high-avidity T-cell clones recognize the immunodominant pp65 peptide antigen pp65495,503 (NLVPMVATV) presented by the major histocompatibility complex (MHC) molecule HLA-A2 in a similar manner, several public high-affinity T-cell receptors (TCRs) specific for the pp65495,503,HLA-A2 complex have been investigated. Expression, purification and crystallization were performed and preliminary crystallographic data were collected to 4.7,┼ resolution for the RA15 TCR in complex with the pp65495,503,HLA-A2 complex. Comparison of the RA15,pp65495,503,HLA-A2 complex molecular-replacement solution with the structure of another high-affinity pp65495,503,HLA-A2-specific TCR, RA14, shows a shared docking mode, indicating that the clonal focusing could be accompanied by the selection of a most favoured peptide-readout mode. However, the position of the RA15 V, domain is significantly shifted, suggesting a different interatomic interaction network. [source]


Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2009
Marc Bailly
Thermus thermophilus deprived of asparagine synthetase synthesizes Asn on tRNAAsnvia a tRNA-dependent pathway involving a nondiscriminating aspartyl-tRNA synthetase that charges Asp onto tRNAAsn prior to conversion of the Asp to Asn by GatCAB, a tRNA-dependent amidotransferase. This pathway also constitutes the route of Asn-tRNAAsn formation by bacteria and archaea deprived of asparaginyl-tRNA synthetase. The partners involved in tRNA-dependent Asn formation in T. thermophilus assemble into a ternary complex called the transamidosome. This particule produces Asn-tRNAAsn in the presence of free Asp, ATP and an amido-group donor. Crystals of the transamidosome from T. thermophilus were obtained in the presence of PEG 4000 in MES,NaOH buffer pH 6.5. They belonged to the primitive monoclinic space group P21, with unit-cell parameters a = 115.9, b = 214.0, c = 127.8,┼, , = 93.3░. A complete data set was collected to 3,┼ resolution. Here, the isolation and crystallization of the transamidosome from T. thermophilus and preliminary crystallographic data are reported. [source]