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Structure determination of feline panleukopenia virus empty particles
Author(s) -
Agbandje Mavis,
McKenna Robert,
Rossmann Michael G,
Strassheim M. Lisa,
Parrish Colin R
Publication year - 1993
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.340160204
Subject(s) - canine parvovirus , orthorhombic crystal system , crystallography , resolution (logic) , capsid , parvovirus , virus , virology , chemistry , hemagglutination , biology , physics , microbiology and biotechnology , crystal structure , artificial intelligence , computer science
Various crystal forms of the single‐stranded DNA, feline panleukopenia virus (FPV), a parvovirus, have been grown of both full virions and empty particles. The structure of empty particles crystallized in an orthorhombic space group P 2 1 2 1 2 1 , with unit cell dimensions a = 380.1 Å, b = 379.3 Å, and c = 350.9 Å, has been determined to 3.3 Å resolution. The data were collected using oscillation photography with synchrotron radiation. The orientations of the empty capsids in the unit cell were determined using a self‐rotation function and their positions were obtained with an R ‐factor search using canine parvovirus (CPV) as a model. Phases were then calculated, based on the CPV model, to 6.0 Å resolution and gradually extended to 3.3 Å resolution by molecular replacement electron density averaging. The resultant electron density was readily interpreted in terms of the known amino acid sequence. The structure is contrasted to that of CPV in terms of host range, neutralization by antibodies, hemagglutination properties, and binding of genomic DNA. © Wiley‐Liss, Inc.