
pmid: 8392729
AbstractVarious 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 P212121, 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.
Protein Conformation, Hemagglutination, Molecular Sequence Data, Virion, Parvoviridae, DNA-Binding Proteins, Dogs, X-Ray Diffraction, Neutralization Tests, Cats, Animals, Amino Acid Sequence, Feline Panleukopenia Virus, Antigens, Viral, Cells, Cultured
Protein Conformation, Hemagglutination, Molecular Sequence Data, Virion, Parvoviridae, DNA-Binding Proteins, Dogs, X-Ray Diffraction, Neutralization Tests, Cats, Animals, Amino Acid Sequence, Feline Panleukopenia Virus, Antigens, Viral, Cells, Cultured
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