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Crystallization and preliminary X-ray analysis of cyclophilin from Leishmania donovani
Rahul Banerjee1, Madhuri Dutta, Malabika Sen
1Saha Institute of Nuclear Physics, Sector 1, Block AF, Bidhan Nagar, Kolkata-64, India. surfaces@cmb2.saha.ernet.in
Abstract:
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.