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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.

Original publication

DOI

10.1107/S1744309105008195

Type

Journal article

Journal

Acta crystallographica. Section F, Structural biology and crystallization communications

Publication Date

04/2005

Volume

61

Pages

421 - 423

Addresses

Nuffield Department of Clinical Medicine, John Radcliffe Hospital, Oxford University, Oxford OX3 9DU, England.

Keywords

Inclusion Bodies, Viral, West Nile virus, Viral Envelope Proteins, Crystallization, X-Ray Diffraction, Binding Sites, Protein Structure, Tertiary, Protein Folding, Volatilization