Pb. Rosenthal et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE INFLUENZA-C VIRUS GLYCOPROTEIN, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 1041-1045
Citations number
41
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
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 m
embranes. A bromelain-released soluble form of HEF has been crystalliz
ed. Two different tetragonal forms have been identified from crystals
with the same morphology [P4(1(3))22, a = b = 154.5, c = 414.4 Angstro
m, and P4(1(3))2(1)2, a = b = 217.4, c = 421.4 Angstrom]. Both crystal
forms share a common packing scheme. Synchrotron data collection and
flash cooling of crystals have been used for high-resolution data coll
ection.