Crystallization and preliminary X-ray analysis of the matrix protein from Ebola virus
Crystallization and preliminary X-ray analysis of the matrix protein from Ebola virus
复制标题
DOI：
10.1107/s0907444900004388
复制
发表时间：
2000-06-01
影响因子：
2.2
通讯作者：
Weissenhorn, W
中科院分区：
文献类型：
--
作者：
Dessen, A;Forest, E;Weissenhorn, W
埃博拉病毒的基质蛋白是一种膜相关分子，在病毒出芽中发挥作用。尽管其功能与其他病毒基质蛋白相似，但它没有显示序列相似性，因此可能具有不同的折叠。埃博拉病毒VP 40基质蛋白的X射线衍射质量晶体通过悬滴气相扩散法生长。晶体属于单斜空间群C2，晶胞参数a = 64.4，B = 91.1，c = 47.9埃，β = 96.3度。使用同步辐射收集了1.9埃分辨率的数据集。该晶胞含有一个分子量为35 kDa的分子/不对称单元，相应的体积溶剂含量为35%。
The matrix protein from Ebola virus is a membrane-associated molecule that plays a role in viral budding. Despite its functional similarity to other viral matrix proteins, it displays no sequence similarity and hence may have a distinct fold. X-ray diffraction quality crystals of the Ebola VP40 matrix protein were grown by the hanging-drop vapour-diffusion method. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 64.4, b = 91.1, c = 47.9 Angstrom, beta = 96.3 degrees. A data set to 1.9 Angstrom resolution has been collected using synchrotron radiation. The unit cell contains one molecule of molecular weight 35 kDa per asymmetric unit, with a corresponding volume solvent content of 35%.