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Expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon Thermococcus sibiricus.

机译:从古生球菌嗜热球菌中表达热稳定的短链醇脱氢酶的表达,纯化和结晶。

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摘要

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.
机译:酒精脱氢酶属于氧化还原酶家族,在广泛的生理过程中起着重要作用。它们催化依赖辅因子的醇可逆氧化为相应的醛或酮。来自嗜热古生球菌Thercococcus sibiricus的NADP依赖的短链醇脱氢酶TsAdh319被过表达,纯化和结晶。使用悬滴蒸汽扩散法,使用25%(w / v)聚乙二醇3350 pH 7.5作为沉淀剂获得晶体。晶体衍射至1.68 A的分辨率,属于I222空间群,其晶胞参数a = 55.63,b = 83.25,c = 120.75A。

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