CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE INFLUENZA-C VIRUS GLYCOPROTEIN

Citation
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
ISSN journal
09074449
Volume
52
Year of publication
1996
Part
5
Pages
1041 - 1045
Database
ISI
SICI code
0907-4449(1996)52:<1041:CAPDSO>2.0.ZU;2-H
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 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.