Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus

被引：1
|
作者：
Bong, Seoung Min [1 ]
Moon, Jin Ho [2 ]
Kim, Hwa Young [3 ]
Kim, Hong Seok [4 ]
Chi, Young Min [1 ]
Kim, Augustine Yonghwi [5 ]
机构：
[1] Korea Univ, Div Biotechnol, Coll Life Sci, Seoul 136713, South Korea
[2] Korea Univ, Inst Life Sci & Nat Resources, Seoul 136713, South Korea
[3] Yeungnam Univ, Dept Biochem & Mol Biol, Coll Med, Deagu 705717, South Korea
[4] Univ Texas Hlth Sci Ctr San Antonio, Clin Sci Lab, San Antonio, TX 78229 USA
[5] Sejong Univ, Dept Food Sci, Seoul 143747, South Korea
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2009年 / 65卷
关键词：
METHIONINE SULFOXIDE REDUCTASES; PROTEINS;
D O I：
10.1107/S1744309109037105
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Free methionine-(R)-sulfoxide reductase (fRMsr) catalyzes the reduction of the free form of methionine-(R)-sulfoxide back to free methionine. The fRMsr protein from Staphylococcus aureus was overexpressed in Escherichia coli, purified and crystallized at 295 K using ammonium sulfate as a precipitant. Diffraction data were collected to 1.7 angstrom resolution from a native crystal using synchrotron radiation. The crystal belonged to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 89.84, c = 88.75 angstrom, alpha = beta = 90, gamma = 120 degrees. Assuming the presence of one molecule in the asymmetric unit, the calculated Matthews coefficient value was 2.21 angstrom(3) Da(-1), with a solvent content of 57.1%.
引用
收藏
页码：1120 / 1122
页数：3
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