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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




Journal article


Acta crystallographica. Section F, Structural biology and crystallization communications

Publication Date





421 - 423


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


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