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Updated: Jun 12, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon
A V Lyashenko1, E Y Bezsudnova, V M Gumerov
1Shubnikov Institute of Crystallography, RAS, Leninsky Prospekt 59, Moscow 119333, Russia. lyashenko@ns.crys.ras.ru
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.
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