Refolding, crystallization and preliminary X-ray structural studies of the West Nile virus envelope (E) protein domain III
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چکیده
منابع مشابه
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...
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The putative receptor-binding domain (domain III) of the flavivirus Langat envelope glycoprotein has been crystallized using the hanging-drop vapor-diffusion method at 277 K. Two distinct crystal morphologies were observed to grow under the same conditions. The crystal forms both belong to a trigonal space group, P3(1)21 or P3(2)21, with unit-cell parameters a = 80.93, c = 132.1 A and a = 104.8...
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Using a panel of neutralizing monoclonal antibodies, we have mapped epitopes in domain III of the envelope protein of the New York strain of West Nile virus. The ability of monoclonal antibodies that recognize these epitopes to neutralize virus appeared to differ between lineage I and II West Nile virus strains, and epitopes were located on the upper surface of domain III at residues E307, E330...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2005
ISSN: 1744-3091
DOI: 10.1107/s1744309105008195