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The human C-type lectin-like protein CLEC-2 has recently been shown to be expressed on the surface of platelets and to function as a receptor for the snake-venom protein rhodocytin. The C-type lectin-like domain (CTLD) of CLEC-2 was expressed in Escherichia coli, refolded and purified. Crystals of this recombinant CLEC-2 were grown by sitting-drop vapour diffusion using polyethylene glycol (PEG) 6000 as a precipitant. After optimization, crystals were grown which diffracted to 2.0 A using in-house radiation (lambda = 1.5418 A). These crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 35.407, b = 55.143, c = 56.078 A. The presence of one molecule per asymmetric unit is consistent with a crystal volume per unit weight (VM) of 1.82 A3 Da(-1) and a solvent content of 32.6%. These results suggest that crystals producing diffraction of this quality will be suitable for the structural determination of human CLEC-2.

Original publication

DOI

10.1107/S1744309105037991

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

01/12/2005

Volume

61

Pages

1094 - 1096

Keywords

Blood Platelets, Cloning, Molecular, Crystallization, Crystallography, Crystallography, X-Ray, Escherichia coli, Humans, Lectins, C-Type, Membrane Glycoproteins, Plasmids, Polyethylene Glycols, Protein Folding, Protein Structure, Tertiary, Recombinant Proteins, Solvents, Thrombosis, Viper Venoms, X-Ray Diffraction