Expression, purification, crystalization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei
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.
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| Main Authors: | , , , , , |
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| Format: | Journal Article biblioteca |
| Language: | English |
| Published: |
1998
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| Subjects: | bovinae, trypanosoma brucei, proteins, purification, crystallization, genes, |
| Online Access: | https://hdl.handle.net/10568/27965 |
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