Crystallization and preliminary X-ray crystallographic analysis of the putative NADP(H)-dependent oxidoreductase YncB from Vibrio vulnificus

被引:2
作者
Kim, Min-Kyu [1 ]
An, Young Jun [1 ]
Jeong, Chang-Sook [1 ]
Cha, Sun-Shin [1 ,2 ]
机构
[1] Korea Inst Ocean Sci & Technol, Marine Biotechnol Res Div, Ansan, South Korea
[2] Univ Sci & Technol, Dept Marine Biotechnol, Taejon, South Korea
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2012年 / 68卷
基金
新加坡国家研究基金会;
关键词
MDR superfamily; Vibrio vulnificus; YncB; MEDIUM-CHAIN DEHYDROGENASES/REDUCTASES; QUINONE OXIDOREDUCTASE; ALCOHOL DEHYDROGENASES; MDR SUPERFAMILY; CURCUMIN; FAMILY; TETRAHYDROCURCUMIN; MECHANISM; COMPLEX; RATS;
D O I
10.1107/S1744309112030527
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The yncB gene product from Vibrio vulnificus, which belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily, was crystallized using the microbatch crystallization method at 295 K. Diffraction data sets were collected using synchrotron radiation. Crystals of selenomethionine-substituted YncB protein belonged to space group P212121, with unit-cell parameters a = 90.52, b=91.56, c = 104.79 angstrom. Assuming the presence of two molecules in the asymmetric unit, the solvent content was estimated to be about 57%. Crystals of the YncBNADP(H) complex belonged to space group P41212 or P43212, with unit-cell parameters a = b = 90.14, c = 105.61 angstrom. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 56.42%.
引用
收藏
页码:1098 / 1101
页数:4
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