Expression, purification, crystallization and preliminary X-ray diffraction analysis of conjugated bile salt hydrolase from Bifidobacterium longum

Kumar, R S, Brannigan, J A, Pundle, A, Prabhune, A, Dodson, G G and Suresh, C G (2004) Expression, purification, crystallization and preliminary X-ray diffraction analysis of conjugated bile salt hydrolase from Bifidobacterium longum. Acta Crystallographica Section D: Biological Crystallography. pp. 1665-1667. ISSN 0907-4449

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Abstract

Conjugated bile salt hydrolase (BSH) catalyses the hydrolysis of the amide bond that conjugates bile acids to glycine and to taurine. The BSH enzyme from Bifidobacterium longum was overexpressed in Escherichia coli BL21(DE3), purified and crystallized. Crystallization conditions were screened using the hanging-drop vapour-diffusion method. Crystal growth, with two distinct morphologies, was optimal in experiments carried out at 303 K. The crystals belong to the hexagonal system, space group P622 with unit-cell parameters a = b = 124.86, c = 219.03 Angstrom, and the trigonal space group P321, with unit-cell parameters a = b = 125.24, c = 117.03 Angstrom. The crystals diffracted X-rays to 2.5 Angstrom spacing. Structure determination using the multiple isomorphous replacement method is in progress.

Item Type:	Article
Copyright, Publisher and Additional Information:	Copyright © 2004 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?za5064
Institution:	The University of York
Academic Units:	The University of York > Chemistry (York)
Depositing User:	Sherpa Assistant
Date Deposited:	11 May 2005
Last Modified:	16 Oct 2014 12:52
Published Version:	http://dx.doi.org/10.1107/S0907444904017561
Status:	Published
Refereed:	Yes
Related URLs:	http://www.iucr.org/cgi-bin/paper?za5064
URI:	http://eprints.whiterose.ac.uk/id/eprint/459