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

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

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 [P41(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.

Original languageEnglish
Pages (from-to)1041-1045
Number of pages5
JournalActa Crystallographica Section D: Biological Crystallography
Volume52
Issue number5
DOIs
StatePublished - 1996

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