Open AccessExpression, purification, crystallization and preliminary X‐ray diffraction analysis of thioredoxin Trx1 from Saccharomyces cerevisiae
Author(s) -
Zhang Yaru,
Bao Rui,
Zhou CongZhao,
Chen Yuxing
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108004612
Subject(s) - saccharomyces cerevisiae , thioredoxin , crystallization , cytosol , chemistry , crystal (programming language) , yeast , biochemistry , gene isoform , crystallography , oxidative stress , enzyme , gene , organic chemistry , programming language , computer science
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 Å resolution. The crystal belongs to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 32.29, b = 46.59, c = 64.20 Å, α = β = γ = 90°.