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Updated: Aug 11, 2026
Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
Published on: April 19, 2016
Refolding, crystallization and preliminary X-ray structural studies of the West Nile virus envelope (E) protein
Fang Yuan1, Zhiyong Lou, Xiaofeng Li
1Nuffield Department of Clinical Medicine, John Radcliffe Hospital, Oxford University, Oxford OX3 9DU, England.
Abstract:
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.
