title: Crystallization and preliminary X-ray analysis of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum.
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%.
authors.affiliation: Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
authors.forename: Koji
authors.initials: K
authors.lastname: Nishikawa
authors.forename: Yasuhito
authors.initials: Y
authors.lastname: Shomura
authors.forename: Shinji
authors.initials: S
authors.lastname: Kawasaki
authors.forename: Youichi
authors.initials: Y
authors.lastname: Niimura
authors.forename: Yoshiki
authors.initials: Y
authors.lastname: Higuchi
mesh_terms: D003001:Cloning, Molecular; D046969:Clostridium acetobutylicum / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry*
chemical_list: C023091:rubredoxin-NAD+ reductase; D009247:NADH, NADPH Oxidoreductases