Crystallization and preliminary X-ray analysis of cyclophilin from Leishmania donovani

Cyclophilin from the parasite Leishmania donovani is a protein with peptidylprolyl cis±trans isomerase activity, in addition to being a receptor for the drug cyclosporin. Crystals of the enzyme have been obtained in space group P43212, with unit-cell parameters a = b = 48.73, c = 140.93 A Ê , and diffract to 3.5 A Ê resolution. One molecule per asymmetric unit gives a solvent content and Matthews coef®cient of 46% and 2.3 A Ê 3 Da ÿ1, respectively. Molecular-replacement calculations with human cyclophilin A as the search model give an unambiguous solution in rotation and translation functions

Crystal structure of cyclophilin from Leishmania donovani at 3.5 Å resolution

The crystal structure of cyclophilin from Leishmania donovani has been solved at 3.5 Å resolution. The protein with peptidylprolyl cis-trans isomerase activity is also a receptor for the drug, cyclosporin. The crystal structure of cyclophilin obtained in space group P43212 with cell parameters a = b =48.73 Å, c = 140.93 Å and one molecule in the asymmetric unit, was solved by molecular replacement using human cyclophilin A as the search model. The refined low resolution structure (R = 0.218 and /Rfree = 0.324) clearly indicates the conservation of the cyclosporin binding-site geometry with respect to human cyclophilin A