来自假结核耶尔森菌的硫醇过氧化物酶的表达、纯化、结晶及初步X射线衍射分析。
Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis.
作者信息
Gabrielsen Mads, Zetterström Caroline E, Wang Dai, Beckham Katherine S H, Elofsson Mikael, Isaacs Neil W, Roe Andrew J
机构信息
Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, Glasgow Biomedical Research Centre, Glasgow G12 8QQ, Scotland.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1606-9. doi: 10.1107/S1744309110039679. Epub 2010 Nov 25.
Abstract
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.
摘要
硫醇过氧化物酶是一种非典型的2-半胱氨酸过氧化物酶，可还原烷基过氧化氢。野生型和C61S突变体蛋白已在大肠杆菌中重组表达，并通过镍亲和色谱法进行纯化。最初的结晶试验在有和没有二硫苏糖醇（DTT）的情况下，在三种不同的空间群（P2(1)、P6(4)和P2(1)2(1)2(1)）中产生了三种晶体形式。
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