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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):23-5. doi: 10.1107/S1744309109047162. Epub 2009 Dec 25.

Crystallization and preliminary X-ray analysis of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum.

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1
Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.

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%.

PMID:
20057062
PMCID:
PMC2805528
DOI:
10.1107/S1744309109047162
[Indexed for MEDLINE]
Free PMC Article
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