Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor
The human C-type lectin-like protein CLEC5A (also known as MDL-1) is expressed on the surface of myeloid cells and plays a critical role in dengue-virus-induced disease by signalling through the transmembrane adaptor protein DAP12. The C-type lectin-like domain of CLEC5A was expressed in Escherichia...
| Asıl Yazarlar: | , |
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| Materyal Türü: | Journal article |
| Dil: | English |
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2009
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| _version_ | 1826275999250120704 |
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| author | Watson, A Ocallaghan, C |
| author_facet | Watson, A Ocallaghan, C |
| author_sort | Watson, A |
| collection | OXFORD |
| description | The human C-type lectin-like protein CLEC5A (also known as MDL-1) is expressed on the surface of myeloid cells and plays a critical role in dengue-virus-induced disease by signalling through the transmembrane adaptor protein DAP12. The C-type lectin-like domain of CLEC5A was expressed in Escherichia coli, refolded and purified. Recombinant CLEC5A crystals were grown by sitting-drop vapour diffusion using polyethylene glycol 6000 as a precipitant. After optimization, crystals were grown which diffracted to 1.56 Å using synchrotron radiation. The results presented in this paper suggest that crystals producing diffraction of this quality will be suitable for structural determination of human CLEC5A. © 2010 International Union of Crystallography All rights reserved. |
| first_indexed | 2024-03-06T23:07:22Z |
| format | Journal article |
| id | oxford-uuid:644f88e0-c158-44d6-95db-d8860c9de2f6 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:07:22Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:644f88e0-c158-44d6-95db-d8860c9de2f62022-03-26T18:18:09ZCrystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptorJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:644f88e0-c158-44d6-95db-d8860c9de2f6EnglishSymplectic Elements at Oxford2009Watson, AOcallaghan, CThe human C-type lectin-like protein CLEC5A (also known as MDL-1) is expressed on the surface of myeloid cells and plays a critical role in dengue-virus-induced disease by signalling through the transmembrane adaptor protein DAP12. The C-type lectin-like domain of CLEC5A was expressed in Escherichia coli, refolded and purified. Recombinant CLEC5A crystals were grown by sitting-drop vapour diffusion using polyethylene glycol 6000 as a precipitant. After optimization, crystals were grown which diffracted to 1.56 Å using synchrotron radiation. The results presented in this paper suggest that crystals producing diffraction of this quality will be suitable for structural determination of human CLEC5A. © 2010 International Union of Crystallography All rights reserved. |
| spellingShingle | Watson, A Ocallaghan, C Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor |
| title | Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor |
| title_full | Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor |
| title_fullStr | Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor |
| title_full_unstemmed | Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor |
| title_short | Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor |
| title_sort | crystallization and x ray diffraction analysis of human clec5a mdl 1 a dengue virus receptor |
| work_keys_str_mv | AT watsona crystallizationandxraydiffractionanalysisofhumanclec5amdl1adenguevirusreceptor AT ocallaghanc crystallizationandxraydiffractionanalysisofhumanclec5amdl1adenguevirusreceptor |