Expression, purification, crystallization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei.

TitleExpression, purification, crystallization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei.
Publication TypeJournal Article
Year of Publication1998
AuthorsDao-Thi, M-H., T. R. Transue, R. Pellé, N. B. Murphy, F. Poortmans, and J. Steyaert
JournalActa Crystallogr D Biol Crystallogr
Volume54
IssuePt 5
Pagination1046-8
Date Published1998 Sep 1
ISSN0907-4449
KeywordsAnimals, Crystallization, Crystallography, X-Ray, Peptidylprolyl Isomerase, Protein Conformation, Protozoan Proteins, Trypanosoma brucei brucei
Abstract

Cyclophilin A from the bovine parasite Trypanosoma brucei brucei has been cloned, expressed in Escherichia coli, purified and crystallized in the presence of cyclosporin A using ammonium sulfate as a precipitant. The crystals belong to the orthorhombic crystal system with unit-cell dimensions of a = 118.61, b = 210.15 and c = 153.21 A. A data set complete to 2.7 A has been collected using rotating-anode radiation, however the crystals diffract to at least 2.1 A resolution using synchrotron radiation.

Alternate JournalActa Crystallogr. D Biol. Crystallogr.
PubMed ID9757134