Refolding, crystallization and preliminary X-ray structural studies of the West Nile virus envelope (E) protein domain III.
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 P222(1), with unit-cell parameters a = 52.6, b = 59.7, c = 95.0 A. A complete data set was collected to 2.8 A at 100 K with Cu Kalpha X-rays from a rotating-anode generator.
Yuan
Fang
F
Nuffield Department of Clinical Medicine, John Radcliffe Hospital, Oxford University, Oxford OX3 9DU, England.
Lou
Zhiyong
Z
Li
Xiaofeng
X
Chen
Yu Wai
YW
Bell
John I
JI
Rao
Zihe
Z
Gao
George F
GF
D001665:Binding Sites; D003460:Crystallization / Q000379:methods; D007181:Inclusion Bodies, Viral; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D014759:Viral Envelope Proteins / Q000737:chemistry*; D014835:Volatilization; D014902:West Nile virus / Q000737:chemistry*; D014961:X-Ray Diffraction
D014759:Viral Envelope Proteins