Open AccessCrystallization and X‐ray diffraction analysis of human CLEC5A (MDL‐1), a dengue virus receptor
Author(s) -
Watson Aleksandra A.,
O'Callaghan Christopher A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109047915
Subject(s) - crystallization , polyethylene glycol , recombinant dna , dengue virus , escherichia coli , diffraction , x ray crystallography , virus , biophysics , biology , crystallography , chemistry , materials science , virology , biochemistry , optics , gene , organic chemistry , physics
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.