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

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JournalActa Crystallographica Section D: Biological Crystallography
DatePublished - Sep 2004
Issue number9
Volume60
Number of pages3
Pages (from-to)1665-1667
Original languageEnglish

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.

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Copyright © 2004 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?za5064

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