These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Expression, purification, crystallization and preliminary X-ray diffraction analysis of conjugated bile salt hydrolase from Bifidobacterium longum.
    Author: Kumar RS, Brannigan JA, Pundle A, Prabhune A, Dodson GG, Suresh CG.
    Journal: Acta Crystallogr D Biol Crystallogr; 2004 Sep; 60(Pt 9):1665-7. PubMed ID: 15333949.
    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 A, and the trigonal space group P321, with unit-cell parameters a = b = 125.24, c = 117.03 A. The crystals diffracted X-rays to 2.5 A spacing. Structure determination using the multiple isomorphous replacement method is in progress.
    [Abstract] [Full Text] [Related] [New Search]