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Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor
Aleksandra A Watson1, Christopher A O'Callaghan
1Henry Wellcome Building of Molecular Physiology, University of Oxford, Roosevelt Drive, Oxford, England.
None:
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 A 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.
