Crystallization and X‐ray diffraction analysis of human CLEC‐2

E-ISSN： 1744-3091|61|12|1094-1096

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.61, Iss.12, 2005-12, pp. : 1094-1096

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Abstract

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 Å using in‐house radiation (λ = 1.5418 Å). These crystals belonged to the orthorhombic space group P2₁2₁2₁, with unit‐cell parameters a = 35.407, b = 55.143, c = 56.078 Å. The presence of one molecule per asymmetric unit is consistent with a crystal volume per unit weight (V_M) of 1.82 Å³ 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.