Expression, purification, crystallization and preliminary X-ray diffraction analysis of thioredoxin Trx1 from Saccharomyces cerevisiae.

Expression, purification, crystallization and preliminary X-ray diffraction analysis of thioredoxin Trx1 from Saccharomyces cerevisiae.
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DOI:
10.1107/s1744309108004612
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发表时间:
2008-04
期刊:
Acta crystallographica. Section F, Structural biology and crystallization communications
影响因子:
--
通讯作者:
Yaru Zhang;R. Bao;Cong-Zhao Zhou;Yuxing Chen
Yaru Zhang;R. Bao;Cong-Zhao Zhou;Yuxing Chen
中科院分区:
其他
文献类型:
--
作者:
Yaru Zhang;R. Bao;Cong-Zhao Zhou;Yuxing Chen

文献摘要

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硫氧还蛋白在细胞对氧化应激的反应中起关键作用。已在酿酒酵母中鉴定出三种硫氧还蛋白亚型:两种为胞质型(Trx 1和Trx 2),一种为线粒体型(Trx 3)。在本工作中,胞质形式Trx 1的克隆,表达,纯化和结晶。晶体通过悬滴气相扩散法获得。从单晶收集数据集至1.7 A分辨率。晶体属于空间群P2(1)2(1)2(1),晶胞参数a = 32.29,B = 46.59,c = 64.20,α = β = γ = 90度。
Thioredoxins play key roles in the cellular response to oxidative stress. Three isoforms of thioredoxin have been identified in Saccharomyces cerevisiae: two that are cytosolic (Trx1 and Trx2) and one that is mitochondrial (Trx3). In the present work, the cytosolic form Trx1 was cloned, expressed, purified and crystallized. Crystals were obtained by the hanging-drop vapour-diffusion method. A data set was collected from a single crystal to 1.7 A resolution. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 32.29, b = 46.59, c = 64.20 A, alpha = beta = gamma = 90 degrees .