Crystallization and preliminary X-ray analysis of the matrix protein from Ebola virus

被引:18
作者
Dessen, A
Forest, E
Volchkov, V
Dolnik, O
Klenk, HD
Weissenhorn, W
机构
[1] European Mol Biol Lab, F-38000 Grenoble, France
[2] Inst Biol Struct Jean Pierre Ebel, F-38027 Grenoble, France
[3] Inst Virol, D-35037 Marburg, Germany
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷
关键词
D O I
10.1107/S0907444900004388
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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%.
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页码:758 / 760
页数:3
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