Crystallization and X-ray analysis of d-threonine aldolase from Chlamydomonas reinhardtii
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 Å 3 Da − 1 and the solvent content was 41.9%.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Hirato, Y. Goto, M. Tokuhisa, M. Tanigawa, M. Nishimura, K. Tags: d-threonine aldolase Chlamydomonas reinhardtii d-amino acids crystallization research communications Source Type: research
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