Crystallization and preliminary X-ray diffraction studies of the influenza C virus glycoprotein.

Abstract

Influenza C virus contains a single surface glycoprotein in its lipid envelope which is the hemagglutinin-esterase-fusion glycoprotein (HEF). HEF binds cell-surface receptors, is a receptor-destroying enzyme (a 9-O-acetylesterase), and mediates the fusion of virus and host cell membranes. A bromelain-released soluble form of HEF has been crystallized. Two different tetragonal forms have been identified from crystals with the same morphology [P(1(3))22, a = b = 154.5, c = 414.4 A, and P4(1(3))2(1)2, a = b = 217.4, c = 421.4 A]. Both crystal forms share a common packing scheme. Synchrotron data collection and flash cooling of crystals have been used for high-resolution data collection.

Cite this paper

@article{Rosenthal1996CrystallizationAP, title={Crystallization and preliminary X-ray diffraction studies of the influenza C virus glycoprotein.}, author={Pierre Rosenthal and F Formanowski and A C Treharne and Julie Newman and John J. Skehel and Herbert Meier-Ewert and Don C. Wiley}, journal={Acta crystallographica. Section D, Biological crystallography}, year={1996}, volume={52 Pt 5}, pages={1041-5} }