| Literature DB >> 20057062 |
Koji Nishikawa1, Yasuhito Shomura, Shinji Kawasaki, Youichi Niimura, Yoshiki Higuchi.
Abstract
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 P4(1)22 or P4(3)22, with unit-cell parameters a = b = 98.6, c = 88.3 A, and diffracted to 2.1 A resolution. Assuming that the crystals contained one molecule per asymmetric unit, the Matthews coefficient was calculated to be 2.7 A(3) Da(-1) and the solvent content to be 54.1%.Entities:
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Year: 2009 PMID: 20057062 PMCID: PMC2805528 DOI: 10.1107/S1744309109047162
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091