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Literature summary for 3.4.21.83 extracted from

  • Rea, D.; Hazell, C.; Andrews, N.W.; Morty, R.E.; Fueloep, V.
    Expression, purification and preliminary crystallographic analysis of oligopeptidase B from Trypanosoma brucei (2006), Acta Crystallogr. Sect. F, 62, 808-810.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
Oligopeptidase B is overexpressed in Escherichia coli as an N-terminally hexahistidine-tagged fusion protein Trypanosoma brucei

Crystallization (Commentary)

Crystallization (Comment) Organism
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 A resolution are collected using synchrotron radiation. The crystals belong to space group P3121 or P3221, with unit-cell parameters a = b = 124.5, c = 249.9 A. A complete data set to 2.7 A is collected using synchrotron radiation Trypanosoma brucei

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei
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-
-

Purification (Commentary)

Purification (Comment) Organism
purified by using metal-affinity chromatography Trypanosoma brucei

Synonyms

Synonyms Comment Organism
oligopeptidase B
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Trypanosoma brucei