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

Citation

Acta Crystallographica - Section D - Biological Crystallography;54: 1046-1048

Authors

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