Open AccessPreliminary X‐ray crystallographic analysis of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans
Author(s) -
Zhang Yanfei,
Cherney Maia M.,
Solomonson Matthew,
Liu Jianshe,
James Michael N. G.,
Weiner Joel H.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109027535
Subject(s) - acidithiobacillus ferrooxidans , crystallography , sulfide , materials science , chemistry , metallurgy , bioleaching , copper
The gene product of open reading frame AFE_1293 from Acidithiobacillus ferrooxidans ATCC 23270 is annotated as encoding a sulfide:quinone oxidoreductase, an enzyme that catalyses electron transfer from sulfide to quinone. Following overexpression in Escherichia coli , the enzyme was purified and crystallized using the hanging‐drop vapour‐diffusion method. The native crystals belonged to the tetragonal space group P 4 2 2 1 2, with unit‐cell parameters a = b = 131.7, c = 208.8 Å, and diffracted to 2.3 Å resolution. Preliminary crystallographic analysis indicated the presence of a dimer in the asymmetric unit, with an extreme value of the Matthews coefficient ( V M ) of 4.53 Å 3 Da −1 and a solvent content of 72.9%.