Expression, purification, crystallization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei.
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.
Dao-Thi
M H
MH
Dienst Ultrastrutuur, Vlaams Interuniversitair Instituut Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B-1640 Sint-Genesius-Rode, Belgium.
Transue
T R
TR
Pellé
R
R
Murphy
N B
NB
Poortmans
F
F
Steyaert
J
J
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D015800:Protozoan Proteins / Q000737:chemistry* / Q000302:isolation & purification; D014346:Trypanosoma brucei brucei / Q000737:chemistry*
D015800:Protozoan Proteins; D019696:Peptidylprolyl Isomerase