TY - JOUR
T1 - Expression, purification, crystallization and preliminary X-ray studies of the Ebola VP35 interferon inhibitory domain
AU - Leung, Daisy W.
AU - Ginder, Nathaniel D.
AU - Nix, Jay C.
AU - Basler, Christopher F.
AU - Honzatko, Richard B.
AU - Amarasinghe, Gaya K.
PY - 2009
Y1 - 2009
N2 - 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.
AB - 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.
KW - Antiviral antagonists
KW - Ebola VP35
KW - Interferon inhibitory domain
UR - http://www.scopus.com/inward/record.url?scp=59749097573&partnerID=8YFLogxK
U2 - 10.1107/S1744309108044187
DO - 10.1107/S1744309108044187
M3 - Article
C2 - 19194011
AN - SCOPUS:59749097573
SN - 1744-3091
VL - 65
SP - 163
EP - 165
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 2
ER -