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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt 2):163-5. doi: 10.1107/S1744309108044187. Epub 2009 Jan 31.

Expression, purification, crystallization and preliminary X-ray studies of the Ebola VP35 interferon inhibitory domain.

Author information

1
Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.

Abstract

Ebola VP35 is a multifunctional protein that is important for host immune suppression and pathogenesis. VP35 contains an N-terminal oligomerization domain and a C-terminal interferon inhibitory domain (IID). Mutations within the VP35 IID result in loss of host immune suppression. Here, efforts to crystallize recombinantly overexpressed VP35 IID that was purified from Escherichia coli are described. Native and selenomethionine-labeled crystals belonging to the orthorhombic space group P2(1)2(1)2(1) were obtained by the hanging-drop vapor-diffusion method and diffraction data were collected at the ALS synchrotron.

PMID:
19194011
PMCID:
PMC2635856
DOI:
10.1107/S1744309108044187
[Indexed for MEDLINE]
Free PMC Article

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