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

Citation
A. Dessen et al., Crystallization and preliminary X-ray analysis of the matrix protein from Ebola virus, ACT CRYST D, 56, 2000, pp. 758-760
Citations number
21
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
6
Pages
758 - 760
Database
ISI
SICI code
0907-4449(200006)56:<758:CAPXAO>2.0.ZU;2-M
Abstract
The matrix protein from Ebola virus is a membrane-associated molecule that plays a role in viral budding. Despite its functional similarity to other v iral matrix proteins, it displays no sequence similarity and hence may have a distinct fold. X-ray diffraction quality crystals of the Ebola VP40 matr ix protein were grown by the hanging-drop vapour-diffusion method. The crys tals 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 uni t cell contains one molecule of molecular weight 35 kDa per asymmetric unit , with a corresponding volume solvent content of 35%.