Crystallization of the reovirus type 3 Dearing core. Crystal packing is determined by the lambda 2 protein.
Core particles of reovirus type 3 Dearing (T3D) crystallized in the face-centered cubic space group F432 with dimensions of 1270 A along each edge of the unit cell. Core particles of reovirus type 1 Lang (T1L) did not crystallize. Experiments with core particles derived from 27 different T1L x T3D reassortant viruses indicated that the L2 genome segment determined the capacity of cores to crystallize. This finding indicates important differences in the surface topography of the L2-translation product, the lambda 2 protein, of these two isolates, and suggests that important crystal contacts are mediated by this protein. These data are used to generate a model of the packing of reovirus core particles within the unit cell.
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.
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Coombs
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Fields
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Harrison
D003460:Crystallization; D005814:Genes, Viral; D012089:Mammalian orthoreovirus 3 / Q000235:genetics*; D008958:Models, Molecular; D011487:Protein Conformation; D012087:Reoviridae / Q000235:genetics*; D014758:Viral Core Proteins / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
D014758:Viral Core Proteins