TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction studies of the influenza C virus glycoprotein
AU - Rosenthal, P. B.
AU - Formanowski, F.
AU - Treharne, A. C.
AU - Newman, J.
AU - Skehel, J. J.
AU - Meier-Ewert, H.
AU - Wiley, D. C.
PY - 1996
Y1 - 1996
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0030500468&partnerID=8YFLogxK
U2 - 10.1107/S0907444996005021
DO - 10.1107/S0907444996005021
M3 - Article
AN - SCOPUS:0030500468
SN - 0907-4449
VL - 52
SP - 1041
EP - 1045
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 5
ER -