Banerjee, R. ; Dutta, M. ; Sen, M. ; Datta, A. K. (2002) Crystallization and preliminary X-ray analysis of cyclophilin from Leishmania donovani Acta Crystallographica Section D, 58 . pp. 1846-1847. ISSN 0907-4449
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Official URL: http://scripts.iucr.org/cgi-bin/paper?pu0056
Related URL: http://dx.doi.org/10.1107/S0907444902012611
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 P43212, with unit-cell parameters a = b = 48.73, c = 140.93 Å, and diffract to 3.5 Å resolution. One molecule per asymmetric unit gives a solvent content and Matthews coefficient of 46% and 2.3 Å3 Da-1, respectively. Molecular-replacement calculations with human cyclophilin A as the search model give an unambiguous solution in rotation and translation functions.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to International Union of Crystallography. |
| Keywords: | Cyclophilin |
| ID Code: | 86515 |
| Deposited On: | 10 Mar 2012 12:55 |
| Last Modified: | 10 Mar 2012 12:55 |
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