Reference - Detail
|Author||Hirato Y, Goto M, Tokuhisa M, Tanigawa M, Nishimura K.|
|Title||Crystallization and X-ray analysis of D-threonine aldolase from Chlamydomonas reinhardtii.|
|Journal||Acta Crystallogr F Struct Biol Commun|
D-Threonine aldolase from the green alga Chlamydomonas reinhardtii (CrDTA) catalyzes the interconversion of several β-hydroxy-D-amino acids (e.g. D-threonine) and glycine plus the corresponding aldehydes. Recombinant CrDTA was overexpressed in Escherichia coli and purified to homogeneity; it was subsequently crystallized using the hanging-drop vapour-diffusion method at 295 K. Data were collected and processed at 1.85 Å resolution. Analysis of the diffraction pattern showed that the crystal belonged to space group P1, with unit-cell parameters a = 64.79, b = 74.10, c = 89.94 Å, α = 77.07, β = 69.34, γ = 71.93°. The asymmetric unit contained four molecules of CrDTA. The Matthews coefficient was calculated to be 2.12 Å3 Da-1 and the solvent content was 41.9%.
|MeSH||Algal Proteins / chemistry* Algal Proteins / genetics Algal Proteins / metabolism Amino Acid Sequence Chlamydomonas reinhardtii / chemistry* Chlamydomonas reinhardtii / enzymology Cloning, Molecular Crystallization Crystallography, X-Ray Escherichia coli / genetics Escherichia coli / metabolism Gene Expression Glycine Hydroxymethyltransferase / chemistry* Glycine Hydroxymethyltransferase / genetics Glycine Hydroxymethyltransferase / metabolism Plasmids / chemistry Plasmids / metabolism Recombinant Proteins / chemistry Recombinant Proteins / genetics Recombinant Proteins / metabolism X-Ray Diffraction|
|WOS Category||BIOCHEMICAL RESEARCH METHODS BIOCHEMISTRY & MOLECULAR BIOLOGY BIOPHYSICS CRYSTALLOGRAPHY|