Published in

International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 6(66), p. 655-657, 2010

DOI: 10.1107/s1744309110002654

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 2010 by A. V. Lyashenko, E. Y. Bezsudnova, V. M. Gumerov ORCID, A. A. Lashkov, A. V. Mardanov, A. M. Mikhailov, K. M. Polyakov, V. O. Popov, N. V. Ravin, K. G. Skryabin, V. K. Zabolotniy, T. N. Stekhanova, M. V. Kovalchuk
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

Full text: Unavailable

Green circle
Preprint: archiving allowed
Upload
Green circle
Postprint: archiving allowed
Upload
Green circle
Published version: archiving allowed
Upload
Policy details
Data provided by SHERPA/RoMEO

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.