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来自澳大拉西亚滑螯虾的La1的结晶及初步X射线衍射研究。

Crystallization and preliminary X-ray diffraction studies of La1 from Liocheles australasiae.

作者信息

Kamachi Saori, Nagao Junya, Miyashita Masahiro, Nakagawa Yoshiaki, Miyagawa Hisashi, Tada Toshiji

机构信息

Graduate School of Science, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.

Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.

出版信息

Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):915-7. doi: 10.1107/S2053230X14010589. Epub 2014 Jun 18.

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%.

摘要

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%。

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