Journal article

Publication year: 2006

Pages: 808-810

Journal: Acta Crystallographica Section F: Structural Biology Communications

Volume number: 62

eISSN: 2053-230X

Open access status: Hybrid

DOI Link: https://doi.org/10.1107/S1744309106027874

Publisher: International Union of Crystallography

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.

Harvard Citation style: Rea, D., Hazell, C., Andrews, N., Morty, R. and Fulop, V. (2006) Expression, purification and preliminary crystallographic analysis of oligopeptidase B from Trypanosoma brucei, Acta Crystallographica Section F: Structural Biology Communications, 62, pp. 808-810. https://doi.org/10.1107/S1744309106027874

APA Citation style: Rea, D., Hazell, C., Andrews, N., Morty, R., & Fulop, V. (2006). Expression, purification and preliminary crystallographic analysis of oligopeptidase B from Trypanosoma brucei. Acta Crystallographica Section F: Structural Biology Communications. 62, 808-810. https://doi.org/10.1107/S1744309106027874