嗜热栖热菌YT-1中一种参与过氧化物还原的NADH氧化酶的结晶及初步晶体学分析。
Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1.
作者信息
Mac Sweeney A, D'Arcy A, Higgins T M, Mayhew S G, Toomey D, Walsh M A
机构信息
Department of Chemistry, NUI Galway, Galway, Ireland.
出版信息
Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):297-8. doi: 10.1107/S090744499800941X. Epub 1999 Jan 1.
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 A, and diffract to 2.5 A resolution.
嗜热水栖菌的NADH氧化酶是一种热稳定的黄素酶，其氨基酸序列和其他特性与鼠伤寒沙门氏菌和木聚糖两栖芽孢杆菌的NADH过氧化物酶系统的黄素酶组分相似。该酶已从嗜热水栖菌中分离出来，并采用悬滴气相扩散法，以柠檬酸钠为沉淀剂，在pH 8.5条件下进行结晶。晶体属于六方空间群P622，晶胞参数a = b = 89.9，c = 491.6 Å，衍射分辨率为2.5 Å。
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