Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter

被引:8
作者
Hsu, WH
Chien, FT
Hsu, CL
Wang, TC
Yuan, HS
Wang, WC [1 ]
机构
[1] Natl Chung Hsing Univ, Inst Mol Biol, Taichung 40227, Taiwan
[2] Natl Tsing Hua Univ, Dept Life Sci, Hsinchu, Taiwan
[3] Acad Sinica, Inst Mol Biol, Taipei, Taiwan
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷
关键词
D O I
10.1107/S090744499801525X
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The Agrobacterium radiobacter CCRC 14924 N-carbamyl-D-amino-acid amidohydrolase, the enzyme used for production of D-amino acids, was overexpressed in Escherichia coli JM109. The expressed protein was crystallized by vapour diffusion using lithium sulfate as precipitant. It crystallizes in space group P2(1) with unit-cell parameters cr = 69.8, b = 67.9 and c = 137.8 Angstrom and beta = 96.4 degrees. There are four molecules per asymmetric unit. Crystals diffract to 2.8 Angstrom resolution using a rotating-anode source at cryogenic (113 K) temperatures.
引用
收藏
页码:694 / 695
页数:2
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