Kumar, R S, Brannigan, J A, Pundle, A et al. (3 more authors) (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
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.
|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:||06 Feb 2017 11:35|