Crystallization and preliminary crystallographic analysis of an nadh oxidase that functions in peroxide reduction inthermus aquaticusyt-1
Mac Sweeney, Aengus D'Arcy, Allan Higgins, Timothy M. Mayhew, Stephen G. Toomey, David Walsh, Martin A.
Mac Sweeney, Aengus
D'Arcy, Allan
Higgins, Timothy M.
Mayhew, Stephen G.
Toomey, David
Walsh, Martin A.
Publication Date
1999-01-01
Type
Article
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Citation
Mac Sweeney, Aengus; D'Arcy, Allan; Higgins, Timothy M. Mayhew, Stephen G.; Toomey, David; Walsh, Martin A. (1999). Crystallization and preliminary crystallographic analysis of an nadh oxidase that functions in peroxide reduction inthermus aquaticusyt-1. Acta Crystallographica Section D Biological Crystallography 55 , 297-298
Abstract
NADH oxidase from Thermus aquaticus is a thermostable flavoenzyme that is similar in amino-acid sequence and other properties to the flavoenzyme component of the NADH peroxidase systems from Salmonella typhimurium and Amphibacillus xylanus. The enzyme has been isolated from T. aquaticus and crystallized using the hanging-drop method of vapour diffusion with sodium citrate as a precipitant at pH 8.5. The crystals belong to the hexagonal space group P622 with unit-cell dimensions a = b = 89.9, c = 491.6 Angstrom, and diffract to 2.5 Angstrom resolution.
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Publisher
International Union of Crystallography (IUCr)
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Attribution-NonCommercial-NoDerivs 3.0 Ireland