Open AccessCrystallization and preliminary X‐ray diffraction studies of the influenza C virus glycoprotein
Author(s) -
Rosenthal P. B.,
Formanowski F.,
Treharne A. C.,
Newman J.,
Skehel J. J.,
MeierEwert H.,
Wiley D. C.
Publication year - 1996
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444996005021
Subject(s) - tetragonal crystal system , glycoprotein , chemistry , crystallography , lipid bilayer fusion , hemagglutinin (influenza) , crystallization , virus , membrane , virology , biology , biochemistry , crystal structure , organic chemistry
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 Å, and P 4 1(3) 2 1 2, a = b = 217.4, c = 421.4 Å]. Both crystal forms share a common packing scheme. Synchrotron data collection and flash cooling of crystals have been used for high‐resolution data collection.