Open AccessRefolding, crystallization and preliminary X‐ray structural studies of the West Nile virus envelope (E) protein domain III
Author(s) -
Lou Zhiyong,
Yuan Fang,
Li Xiaofeng,
Chen Yu Wai,
Bell John I.,
Rao Zihe,
Gao George F.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105008195
Subject(s) - crystallization , envelope (radar) , domain (mathematical analysis) , crystallography , west nile virus , structural protein , viral envelope , materials science , virology , chemistry , virus , physics , biology , engineering , thermodynamics , mathematics , telecommunications , mathematical analysis , radar
Domain III of the West Nile virus envelope protein, the putative receptor‐binding domain, is a major virion‐surface determinant for virulence. This protein was reported to be intrinsically unstable and has defied previous crystallization attempts. It has now been purified from inclusion bodies by protein refolding and was crystallized using the hanging‐drop vapour‐diffusion method at 291 K. The crystals belong to space group P 222 1 , with unit‐cell parameters a = 52.6, b = 59.7, c = 95.0 Å. A complete data set was collected to 2.8 Å at 100 K with Cu K α X‐rays from a rotating‐anode generator.