Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis.
Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis.
复制标题
假结核耶尔森菌硫醇过氧化物酶的表达、纯化、结晶和初始 X 射线衍射分析。
DOI:
10.1107/s1744309110039679
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发表时间:
2010
期刊:
影响因子:
--
通讯作者:
Gabrielsen M
中科院分区:
文献类型:
--
作者:
Gabrielsen M
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 (P21, P64 and P212121) both in the presence and the absence of DTT.
影响因子:
5.6
作者:
Hall, Andrea;Sankaran, Banumathi;Poole, Leslie B.;Karplus, P. Andrew
通讯作者:
Karplus, P. Andrew
影响因子:
2.1
作者:
K. Tao
通讯作者:
K. Tao