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

Publication Type:

Journal Article

Authors:

Dao-Thi,M.H.; Transue,T.R.; Pelle,R.; Murphy,N.B.; Poortmans,F.; Steyaert,J.

Source:

Volume 54, Issue Pt 5, p.1046 - 1048 (1998)

URL:

PM:9757134

Keywords:

analysis; Animals; chemistry; Crystallization; Crystallography; X-Ray; Escherichia coli; ESCHERICHIA-COLI; EXPRESSION; isolation & purification; Peptidylprolyl Isomerase; PROTEIN; Protein Conformation; Proteins; Protozoan Proteins; PURIFICATION; Trypanosom

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

Notes:

DA - 19981214
IS - 0907-4449 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Protozoan Proteins)
RN - EC 5.2.1.8 (Peptidylprolyl Isomerase)
SB - IM