Buy article online - an online subscription or single-article purchase is required to access this article.
crystallization communications
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%.