Open AccessCrystallization and preliminary X‐ray diffraction analysis of the metalloregulatory protein DtxR from Thermoplasma acidophilum
Author(s) -
Yeo Hyun Ku,
Kang Jina,
Park Young Woo,
Sung JungSuk,
Lee Jae Young
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111051700
Subject(s) - thermoplasma acidophilum , crystallization , x ray crystallography , crystallography , diffraction , materials science , chemistry , physics , biochemistry , optics , organic chemistry , enzyme
The diphtheria toxin repressor (DtxR) is a metal‐ion‐dependent transcriptional regulator which regulates genes encoding proteins involved in metal‐ion uptake to maintain metal‐ion homeostasis. DtxR from Thermoplasma acidophilum was cloned and overexpressed in Escherichia coli . Crystals of N‐terminally His‐tagged DtxR were obtained by hanging‐drop vapour diffusion and diffracted to 1.8 Å resolution. DtxR was crystallized at 296 K using polyethylene glycol 4000 as a precipitant. The crystals belonged to the orthorhombic space group P 2 1 2 1 2, with unit‐cell parameters a = 61.14, b = 84.61, c = 46.91 Å, α = β = γ = 90°. The asymmetric unit contained approximately one monomer of DtxR, giving a crystal volume per mass ( V M ) of 2.22 Å 3 Da −1 and a solvent content of 44.6%.