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=1...
| Main Authors: | , , , , , |
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| Format: | Journal Article |
| Language: | Inglés |
| Published: |
1998
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| Subjects: | |
| Online Access: | https://hdl.handle.net/10568/27965 |
| _version_ | 1855537184381075456 |
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| author | Dao-Thi, M.H. Transue, T.R. Pelle, Roger Murphy, N.B. Poortmans, F. Steyaert, J. |
| author_browse | Dao-Thi, M.H. Murphy, N.B. Pelle, Roger Poortmans, F. Steyaert, J. Transue, T.R. |
| author_facet | Dao-Thi, M.H. Transue, T.R. Pelle, Roger Murphy, N.B. Poortmans, F. Steyaert, J. |
| author_sort | Dao-Thi, M.H. |
| collection | Repository of Agricultural Research Outputs (CGSpace) |
| description | 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. |
| format | Journal Article |
| id | CGSpace27965 |
| institution | CGIAR Consortium |
| language | Inglés |
| publishDate | 1998 |
| publishDateRange | 1998 |
| publishDateSort | 1998 |
| record_format | dspace |
| spelling | CGSpace279652023-01-28T12:56:17Z Expression, purification, crystalization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei Dao-Thi, M.H. Transue, T.R. Pelle, Roger Murphy, N.B. Poortmans, F. Steyaert, J. bovinae trypanosoma brucei proteins purification crystallization genes 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. 1998 2013-05-06T06:59:38Z 2013-05-06T06:59:38Z Journal Article https://hdl.handle.net/10568/27965 en Limited Access Acta Crystallographica - Section D - Biological Crystallography;54: 1046-1048 |
| spellingShingle | bovinae trypanosoma brucei proteins purification crystallization genes Dao-Thi, M.H. Transue, T.R. Pelle, Roger Murphy, N.B. Poortmans, F. Steyaert, J. Expression, purification, crystalization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei |
| title | Expression, purification, crystalization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei |
| title_full | Expression, purification, crystalization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei |
| title_fullStr | Expression, purification, crystalization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei |
| title_full_unstemmed | Expression, purification, crystalization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei |
| title_short | Expression, purification, crystalization and preliminary X-ray analysis of cyclophilin A from the bovine parasite Trypanosoma brucei brucei |
| title_sort | expression purification crystalization and preliminary x ray analysis of cyclophilin a from the bovine parasite trypanosoma brucei brucei |
| topic | bovinae trypanosoma brucei proteins purification crystallization genes |
| url | https://hdl.handle.net/10568/27965 |
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