Crystallization and preliminary crystallographic investigations of rhodanese from Azotobacter vinelandii

被引:3
作者
Bordo, D
Colnaghi, R
Deriu, D
Carpen, A
Storici, P
Pagani, S
Bolognesi, M
机构
[1] IST, Adv Biotechnol Ctr, I-16132 Genoa, Italy
[2] Univ Genoa, INFM, I-16132 Genoa, Italy
[3] Univ Milan, Dipartimento Sci Mol Agroalimentari, I-20133 Milan, Italy
[4] Univ Milan, CISMI, I-20133 Milan, Italy
[5] Univ Basel, Biozentrum, Div Struct Biol, Basel, Switzerland
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷
关键词
D O I
10.1107/S0907444999006526
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The rhdA gene identified in Azotobacter vinelandii codes for a protein, RhdA, which displays rhodanese (thiosulfate-cyanide sulfurtransferase) activity. RhdA was overexpressed and purified to homogeneity. The protein crystallized in the orthorhombic space group P2(1)2(1)2 with unit-cell parameters a = 44.4, b = 150.8, c = 53.8 Angstrom: on a synchrotron source the diffraction patterns could be collected to a resolution limit of 1.8 Angstrom. Evaluation of the crystal density indicates that the crystal lattice accommodates one molecule per asymmetric unit and that the solvent content is 59% of the total volume.
引用
收藏
页码:1471 / 1473
页数:3
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