Open AccessCrystallization and preliminary X‐ray analysis of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum
Author(s) -
Nishikawa Koji,
Shomura Yasuhito,
Kawasaki Shinji,
Niimura Youichi,
Higuchi Yoshiki
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109047162
Subject(s) - rubredoxin , clostridium acetobutylicum , oxidoreductase , chemistry , crystallization , crystallography , biochemistry , enzyme , butanol , organic chemistry , ethanol
NADH:rubredoxin oxidoreductase (NROR), an O 2 ‐inducible protein, is a versatile electron donor for scavengers of O 2 and reactive oxygen species (ROS) in Clostridium acetobutylicum . Recombinant NROR was overexpressed in Escherichia coli and purified to homogeneity; it was subsequently crystallized using the sitting‐drop vapour‐diffusion method at 293 K. Preliminary crystallographic analysis revealed that the crystals belonged to space group P 4 1 22 or P 4 3 22, with unit‐cell parameters a = b = 98.6, c = 88.3 Å, and diffracted to 2.1 Å resolution. Assuming that the crystals contained one molecule per asymmetric unit, the Matthews coefficient was calculated to be 2.7 Å 3 Da −1 and the solvent content to be 54.1%.