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  • Title: Expression, purification and preliminary crystallographic analysis of oligopeptidase B from Trypanosoma brucei.
    Author: Rea D, Hazell C, Andrews NW, Morty RE, Fülöp V.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2006 Aug 01; 62(Pt 8):808-10. PubMed ID: 16880564.
    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 angstroms 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 angstroms. A complete data set to 2.7 angstroms was collected using synchrotron radiation.
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