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Crystallization and X‐ray analysis of d ‐threonine aldolase from Chlamydomonas reinhardtii
Author(s) -
Hirato Yuki,
Goto Masaru,
Tokuhisa Mayumi,
Tanigawa Minoru,
Nishimura Katsushi
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1602063x
Subject(s) - chlamydomonas reinhardtii , threonine , chlamydomonas , aldolase a , crystallization , chemistry , crystallography , solvent , biochemistry , enzyme , serine , organic chemistry , gene , mutant
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 P 1, 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%.