Abstract
A novel scorpion venom peptide, La1 from Liocheles australasiae, with a molecular weight of 7.8 kDa, is presumed to possess a single von Willebrand factor type C (VWC) domain, a common protein module, based on the position of eight Cys residues in its sequence. The biological function of La1 is still unknown. Deciphering its three-dimensional structure will be helpful in understanding its biological function. La1 was crystallized by the sitting-drop vapour-diffusion method using magnesium sulfate as a precipitant. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a=63.0, b=30.2, c=32.3 Å, β=108.5°, and diffracted to 1.9 Å resolution. The calculated VM based on one molecule per asymmetric unit was 1.87 Å3 Da(-1). The solvent content was 34.1%.
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