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

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.

SUBMITTER: Lyashenko AV 

PROVIDER: S-EPMC2882762 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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

Lyashenko A V AV   Bezsudnova E Y EY   Gumerov V M VM   Lashkov A A AA   Mardanov A V AV   Mikhailov A M AM   Polyakov K M KM   Popov V O VO   Ravin N V NV   Skryabin K G KG   Zabolotniy V K VK   Stekhanova T N TN   Kovalchuk M V MV  

Acta crystallographica. Section F, Structural biology and crystallization communications 20100526 Pt 6

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) polyethyl  ...[more]

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