Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis

被引：5

作者：

Gabrielsen, Mads ^{[1
]}

Zetterstrom, Caroline E. ^{[3
]}

Wang, Dai ^{[1
]}

Beckham, Katherine S. H. ^{[1
]}

Elofsson, Mikael ^{[3
]}

Isaacs, Neil W. ^{[2
]}

Roe, Andrew J. ^{[1
]}

机构：

[1] Glasgow Biomed Res Ctr, Inst Infect Immun & Inflammat, Coll Med Vet & Life Sci, Glasgow G12 8QQ, Lanark, Scotland

[2] Univ Glasgow, Dept Chem, Glasgow G12 8QQ, Lanark, Scotland

[3] Umea Univ, Dept Chem, SE-90187 Umea, Sweden

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

Yersinia pseudotuberculosis; thiol peroxidases; Tpx; peroxiredoxins; ESCHERICHIA-COLI;

D O I：

10.1107/S1744309110039679

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Thiol peroxidase is an atypical 2-Cys peroxiredoxin that reduces alkyl hydroperoxides. Wild-type and C61S mutant protein have been recombinantly expressed in Escherichia coli and purified using nickel-affinity chromatography. Initial crystallization trials yielded three crystal forms in three different space groups (P2(1), P6(4) and P2(1)2(1)2(1)) both in the presence and the absence of DTT.

引用

页码：1606 / 1609

页数：4

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