Kamachi Saori, Nagao Junya, Miyashita Masahiro, Nakagawa Yoshiaki, Miyagawa Hisashi, Tada Toshiji
Graduate School of Science, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.
Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):915-7. doi: 10.1107/S2053230X14010589. Epub 2014 Jun 18.
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%.
一种来自澳链尾蝎的新型蝎毒肽La1,分子量为7.8 kDa,根据其序列中八个半胱氨酸残基的位置推测,它具有一个单一的血管性血友病因子C型(VWC)结构域,这是一种常见的蛋白质模块。La1的生物学功能仍然未知。解析其三维结构将有助于理解其生物学功能。采用坐滴气相扩散法,以硫酸镁作为沉淀剂,使La1结晶。晶体属于单斜空间群C2,晶胞参数a = 63.0、b = 30.2、c = 32.3 Å,β = 108.5°,衍射分辨率为1.9 Å。基于每个不对称单元一个分子计算得到的VM为1.87 Å3 Da-1。溶剂含量为34.1%。