Open AccessCloning, overproduction, purification, crystallization and preliminary X‐ray diffraction analysis of yeast glutaredoxin Grx5
Author(s) -
Wang Yi,
He YongXing,
Yu Jiang,
Zhou CongZhao
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109018417
Subject(s) - saccharomyces cerevisiae , yeast , escherichia coli , biogenesis , crystallization , iron–sulfur cluster , cloning (programming) , overproduction , chemistry , biochemistry , biology , microbiology and biotechnology , gene , enzyme , organic chemistry , computer science , programming language
Grx5 from the yeast Saccharomyces cerevisiae is a monothiol glutaredoxin that is involved in iron–sulfur cluster biogenesis. Here, yeast Grx5 was cloned and overproduced in Escherichia coli . The purified protein was crystallized using the hanging‐drop vapour‐diffusion method. Diffraction data for Grx5 were collected to 1.67 Å resolution. The crystal of Grx5 belonged to space group R 3, with unit‐cell parameters a = b = 85.12, c = 48.95 Å, α = β = 90.00, γ = 120.00°.