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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Watson, Aleksandra A. O'Callaghan, Christopher A.
Description	Country affiliation: United kingdom Author Affiliation: Watson AA ( Henry Wellcome Building of Molecular Physiology, University of Oxford, Roosevelt Drive, Oxford, England.)
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.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
DOI	10.1107/S1744309109047915
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 1
Volume Number	66
Language	English
Publisher	Wiley
Publisher Date	2010-01-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Lectins, C-type Chemistry Receptors, Cell Surface Receptors, Virus Crystallization Crystallography, X-ray
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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

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