Crystallization and X-ray analysis of d-threonine aldolase from Chlamydomonas reinhardtii
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- 作者：Yuki Hirato ; Masaru Goto ; Mayumi Tokuhisa ; Minoru Tanigawa and Katsushi Nishimura
- 关键词：d-threonine aldolase ; Chlamydomonas reinhardtii ; d-amino acids ; crystallization
- 刊名：Acta Crystallographica Section F
- 出版年：2017
- 出版时间：February 2017
- 年：2017
- 卷：73
- 期：2
- 页码：86-89
- 全文大小：370K
- ISSN：1744-3091
文摘
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%.