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Preliminary X‐ray diffraction analysis of crystals of tomato aspermy virus (TAV)
Author(s) -
Canady Mary A.,
Leja Catherine A.,
Day John,
McPherson Alexander
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340210310
Subject(s) - icosahedral symmetry , orthorhombic crystal system , crystallography , capsid , diffraction , resolution (logic) , synchrotron radiation , x ray crystallography , strain (injury) , x ray , virus , chemistry , physics , materials science , crystal structure , optics , virology , biology , artificial intelligence , computer science , anatomy
Tomato aspermy virus (TAV) is a member of the T = 3 cucumovirus group, and the chrysanthemum strain (C‐TAV) has been crystallized in a form suitable for X‐ray structural analysis. The crystals, which grow in 14–17% ethanol at pH 8.5, are of orthorhombic space group I 222 with unit cell dimensions of a = 295.1 Å, b = 320.5 Å, and c = 383.6 Å. There are two T = 3 virus particles in the unit cell, which means that they must be centered at 0,0,0 and 1/2, 1/2, 1/2 with icosahedral 222 symmetry elements coincident with crystallographic symmetry operators. The asymmetric unit of the crystals, therefore, contains one quarter of a virus particle, or 45 capsid subunits. Native diffraction data to 4 Å resolution have been collected using synchrotron radiation, though data appear to be present beyond that resolution. © 1995 Wiley‐Liss, Inc.