Crystallization and preliminary crystallographic analysis of human serine dehydratase

被引：5
|
作者：
Sun, L
Li, XM
Dong, YJ
Yang, MJ
Liu, YW
Han, XQ
Zhang, XE
Pang, H
Rao, ZH [1 ]
机构：
[1] Tsinghua Univ, MOE Prot Sci Lab, Beijing 100084, Peoples R China
[2] Tsinghua Univ, Dept Biol Sci & Biotechnol, Struct Biol Lab, Beijing 100084, Peoples R China
[3] Chinese Acad Sci, Wuhan Inst Virol, Wuhan 430071, Peoples R China
[4] Chinese Acad Sci, Inst Biophys, Natl Lab Macromol, Beijing 100080, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2003年 / 59卷
关键词：
D O I：
10.1107/S0907444903020110
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
L-Serine dehydratase (SDH) catalyzes the pyridoxal phosphate (PLP) dependent deamination of L-serine to yield pyruvate. Recombinant human serine dehydratase was crystallized by the hanging-drop vapour-diffusion method. Crystals were grown at 291 K using (NH(4))(2)SO(4) as precipitant. Diffraction data were obtained to a resolution of 2.5 Angstrom from a single frozen crystal using Cu Kalpha radiation. The crystal belongs to space group I422, with unit-cell parameters a = 157.4, b = 157.4, c = 59.2 Angstrom, alpha = beta = gamma = 90degrees. The asymmetric unit contains one molecule and has a solvent content of about 46%.
引用
收藏
页码：2297 / 2299
页数：3
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