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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.

Original publication

DOI

10.1107/S1744309109047915

Type

Journal article

Journal

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Publication Date

25/12/2009

Volume

66

Pages

29 - 31