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.
复制标题
DOI:
10.1107/s1744309108004612
复制
发表时间:
2008-04
期刊:
影响因子:
--
通讯作者:
Yaru Zhang;R. Bao;Cong-Zhao Zhou;Yuxing Chen
中科院分区:
文献类型:
--
作者:
Yaru Zhang;R. Bao;Cong-Zhao Zhou;Yuxing Chen
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 .