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

Rosenthal P. B. | Zendy; Formanowski F. | Zendy; Treharne A. C. | Zendy; Newman J. | Zendy; Skehel J. J. | Zendy; MeierEwert H. | Zendy; Wiley D. C. | Zendy

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Crystallization 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.

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