来自嗜热栖热球菌的一种耐热短链醇脱氢酶的表达、纯化及结晶
Expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon Thermococcus sibiricus.
作者信息
Lyashenko A V, Bezsudnova E Y, Gumerov V M, Lashkov A A, Mardanov A V, Mikhailov A M, Polyakov K M, Popov V O, Ravin N V, Skryabin K G, Zabolotniy V K, Stekhanova T N, Kovalchuk M V
机构信息
Shubnikov Institute of Crystallography, RAS, Leninsky Prospekt 59, Moscow 119333, Russia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt 6):655-7. doi: 10.1107/S1744309110002654. Epub 2010 May 26.
Abstract
Alcohol dehydrogenases belong to the oxidoreductase family and play an important role in a broad range of physiological processes. They catalyze the cofactor-dependent reversible oxidation of alcohols to the corresponding aldehydes or ketones. The NADP-dependent short-chain alcohol dehydrogenase TsAdh319 from the thermophilic archaeon Thermococcus sibiricus was overexpressed, purified and crystallized. Crystals were obtained using the hanging-drop vapour-diffusion method using 25%(w/v) polyethylene glycol 3350 pH 7.5 as precipitant. The crystals diffracted to 1.68 A resolution and belonged to space group I222, with unit-cell parameters a = 55.63, b = 83.25, c = 120.75 A.
摘要
醇脱氢酶属于氧化还原酶家族，在广泛的生理过程中发挥重要作用。它们催化依赖于辅因子的醇可逆氧化为相应的醛或酮。来自嗜热古菌西伯利亚嗜热栖热菌的NADP依赖型短链醇脱氢酶TsAdh319被过量表达、纯化并结晶。使用悬滴气相扩散法，以25%（w/v）聚乙二醇3350（pH 7.5）作为沉淀剂获得晶体。这些晶体的衍射分辨率为1.68 Å，并属于空间群I222，晶胞参数a = 55.63、b = 83.25、c = 120.75 Å。
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