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Expression, purification and preliminary crystallographic analysis of oligopeptidase B from Trypanosoma brucei

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Rea, Dean, Hazell, Carole, Andrews, Norma W., Morty, Rory E. and Fülöp, Vilmos. (2006) Expression, purification and preliminary crystallographic analysis of oligopeptidase B from Trypanosoma brucei. Acta Crystallographica Section F - Structural Biology and Crystallization Communications, Vol.62 (Part 8). pp. 808-810. ISSN 1744-3091

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Official URL: http://dx.doi.org/10.1107/S1744309106027874

Abstract

African sleeping sickness, also called trypanosomiasis, is a significant cause of morbidity and mortality in sub-Saharan Africa. Peptidases from Trypanosoma brucei, the causative agent, include the serine peptidase oligopeptidase B, a documented virulence factor and therapeutic target. Determination of the three-dimensional structure of oligopeptidase B is desirable to facilitate the development of novel inhibitors. Oligopeptidase B was overexpressed in Escherichia coli as an N-terminally hexahistidine-tagged fusion protein, purified using metal-affinity chromatography and crystallized using the hanging-drop vapour-diffusion technique in 7%(w/v) polyethylene glycol 6000, 1 M LiCl, 0.1 M bis-tris propane pH 7.5. Diffraction data to 2.7 angstrom resolution were collected using synchrotron radiation. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 124.5, c = 249.9 angstrom. A complete data set to 2.7 angstrom was collected using synchrotron radiation.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Faculty of Science > Life Sciences (2010- )
Journal or Publication Title: Acta Crystallographica Section F - Structural Biology and Crystallization Communications
Publisher: Wiley-Blackwell Publishing, Inc.
ISSN: 1744-3091
Date: August 2006
Volume: Vol.62
Number: Part 8
Number of Pages: 3
Page Range: pp. 808-810
Identification Number: 10.1107/S1744309106027874
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
URI: http://wrap.warwick.ac.uk/id/eprint/33269

Data sourced from Thomson Reuters' Web of Knowledge

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