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 P4(3)2(1)2, with unit-cell parameters a = b = 48.73, c = 140.93 A, and diffract to 3.5 A resolution. One molecule per asymmetric unit gives a solvent content and Matthews coefficient of 46% and 2.3 A(3) Da(-1), respectively. Molecular-replacement calculations with human cyclophilin A as the search model give an unambiguous solution in rotation and translation functions.
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D021983:Cyclophilins / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D007893:Leishmania donovani / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D021983:Cyclophilins