Skip to main content
Wiley - PMC COVID-19 Collection logoLink to Wiley - PMC COVID-19 Collection
. 2007 Sep 27;52(5):1041–1045. doi: 10.1107/S0907444996005021

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

P B Rosenthal, F Formanowski, A C Treharne, J Newman, J J Skehel, H Meier‐Ewert, D C Wiley
PMCID: PMC7159800  PMID: 15299621

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 Å, and P41(3)212, 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.


The full text for this article, hosted at http://journals.iucr.org, is unavailable due to technical difficulties.


Articles from Acta Crystallographica Section D: Biological Crystallography are provided here courtesy of Wiley

RESOURCES