Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of glutathionylated Trx1 C33S mutant from yeast
Author(s) -
Lou Xiaochu,
Zhang Yaru,
Bao Rui,
Zhou CongZhao,
Chen Yuxing
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108039316
Subject(s) - saccharomyces cerevisiae , cytosol , mutant , yeast , crystallization , crystallography , biochemistry , biology , chemistry , enzyme , gene , organic chemistry
Thioredoxins (Trxs) are a family of small redox‐active proteins that are found in all living organisms. In Saccharomyces cerevisiae , two cytosolic Trxs (Trx1 and Trx2) and one mitochondrial Trx (Trx3) have previously been identified. In this work, cytosolic Trx1 containing a C33S mutant was overexpressed, purified, glutathionylated and crystallized using the hanging‐drop vapour‐diffusion method. A set of X‐ray diffraction data was collected to 1.80 Å resolution. The crystal belonged to space group P 1, with unit‐cell parameters a = 38.53, b = 38.81, c = 41.70 Å, α = 72.91, β = 87.51, γ = 60.58°.