Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins

Journal Article · Mon Jun 21 04:00:00 EDT 2010 · Acta Crystallogr. F

DOI:https://doi.org/10.1107/S1744309110013266· OSTI ID:1002444

Leung, Daisy W; Borek, Dominika; Farahbakhsh, Mina; Ramanan, Parameshwaran; Nix, Jay C; Wang, Tianjiao; Prins, Kathleen C; Otwinowski, Zbyszek; Honzatko, Richard B; Helgeson, Luke A; Basler, Christopher F; Amarasinghe, Gaya K ^[1]

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1. Texas-HSC

VP35 is one of seven structural proteins encoded by the Ebola viral genome and mediates viral replication, nucleocapsid formation and host immune suppression. The C-terminal interferon inhibitory domain (IID) of VP35 is critical for dsRNA binding and interferon inhibition. The wild-type VP35 IID structure revealed several conserved residues that are important for dsRNA binding and interferon antagonism. Here, the expression, purification and crystallization of recombinant Zaire Ebola VP35 IID mutants R312A, K319A/R322A and K339A in space groups P6{sub 1}22, P2{sub 1}2{sub 1}2{sub 1} and P2{sub 1}, respectively, are described. Diffraction data were collected using synchrotron sources at the Advanced Light Source and the Advanced Photon Source.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1002444
• Journal Information: Acta Crystallogr. F, Journal Name: Acta Crystallogr. F Journal Issue: (6) ; 06, 2010 Vol. 66
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
CRYSTALLIZATION
INHIBITION
INTERFERON
MUTANTS
PROTEINS
PURIFICATION
VIRUSES