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Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase fromPelobacter acetylenicus

Einsle, Oliver, Niessen, Holger, Abt, Dietmar J., Seiffert, Grazyna, Schink, Bernhard, Huber, Robert, Messerschmidt, Albrecht and Kroneck, Peter M. H. 2005. Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase fromPelobacter acetylenicus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 61 (3) , pp. 299-301. 10.1107/S174430910500374X

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Abstract

Acetylene hydratase is a tungsten-containing hydroxylase that converts acetylene to acetaldehyde in a unique reaction that requires a strong reductant. The subsequent disproportionation of acetaldehyde yields acetate and ethanol. Crystals of the tungsten/iron-sulfur protein acetylene hydratase from Pelobacter acetylenicus strain WoAcy 1 (DSM 3246) were grown by the vapour-diffusion method in an N2/H2 atmosphere using polyethylene glycol as precipitant. Growth of crystals suitable for X-ray analysis strictly depended on the presence of TiIII citrate or dithionite as reducing agents.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QR Microbiology
Uncontrolled Keywords: acetylene hydratase; tungsten hydroxylases; oxygen-sensitivity.
Publisher: International Union of Crystallography
ISSN: 1744-3091
Last Modified: 24 Jun 2017 11:00
URI: http://orca-mwe.cf.ac.uk/id/eprint/70001

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