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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.

SUBMITTER: Watson AA

PROVIDER: S-EPMC2805530 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature

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Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1), a dengue virus receptor.

Watson Aleksandra A AA O'Callaghan Christopher A CA

Acta crystallographica. Section F, Structural biology and crystallization communications 20091225 Pt 1

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 dif ...[more]

PMID: 20057064

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