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

Daisy W. Leung, Nathaniel D. Ginder, Jay C. Nix, Christopher F. Basler, Richard B. Honzatko, Gaya K. Amarasinghe

Research output: Contribution to journalArticle

12 Scopus citations

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 P212121 were obtained by the hanging-drop vapor-diffusion method and diffraction data were collected at the ALS synchrotron.

Original languageEnglish
Pages (from-to)163-165
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number2
DOIs
StatePublished - Feb 13 2009
Externally publishedYes

Keywords

  • Antiviral antagonists
  • Ebola VP35
  • Interferon inhibitory domain

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