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

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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 Å resolution and belonged to space group I222, with unit‐cell parameters a = 55.63, b = 83.25, c = 120.75 Å.
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Keywords: alcohol dehydrogenases; archaea; thermostability

Document Type: Research Article

Publication date: June 1, 2010

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