Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticusYT‐1

Autor: Mac Sweeney, Aengus, D'Arcy, Allan, Higgins, Timothy M., Mayhew, Stephen G., Toomey, David, Walsh, Martin A.
Zdroj: Acta Crystallographica Section D: Biological Crystallography; January 1999, Vol. 55 Issue: 1 p297-298, 2p
Abstrakt: NADH oxidase from Thermus aquaticusis a thermostable flavo­enzyme that is similar in amino‐acid sequence and other properties to the flavoenzyme component of the NADH peroxidase systems from Salmonella typhimuriumand Amphibacillus xylanus. The enzyme has been isolated from T. aquaticusand 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 Å, and diffract to 2.5 Å resolution.
Databáze: Supplemental Index