title: Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor.
abstract: 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.
authors.affiliation: Henry Wellcome Building of Molecular Physiology, University of Oxford, Roosevelt Drive, Oxford, England.
authors.forename: Aleksandra A
authors.initials: AA
authors.lastname: Watson
authors.forename: Christopher A
authors.initials: CA
authors.lastname: O'Callaghan
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D037181:Lectins, C-Type / Q000737:chemistry*; D011956:Receptors, Cell Surface / Q000737:chemistry*; D011991:Receptors, Virus / Q000737:chemistry*
chemical_list: C509771:CLEC5A protein, human; D037181:Lectins, C-Type; D011956:Receptors, Cell Surface; D011991:Receptors, Virus; C111476:dengue virus receptor