title: Crystal lattice as biological phenotype for insect viruses.
abstract: Many insect viruses survive for long periods by occlusion within robust crystalline polyhedra composed primarily of a single polyhedrin protein. We show that two different virus families form polyhedra which, despite lack of sequence similarity in the virally encoded polyhedrin protein, have identical cell constants and a body-centered cubic lattice. It is almost inconceivable that this could have arisen by chance, suggesting that the crystal lattice has been preserved because it is particularly well-suited to its function of packaging and protecting viruses.
authors.affiliation: Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
authors.forename: Karin
authors.initials: K
authors.lastname: Anduleit
authors.forename: Geoff
authors.initials: G
authors.lastname: Sutton
authors.forename: Jonathan M
authors.initials: JM
authors.lastname: Diprose
authors.forename: Peter P C
authors.initials: PP
authors.lastname: Mertens
authors.forename: Jonathan M
authors.initials: JM
authors.lastname: Grimes
authors.forename: David I
authors.initials: DI
authors.lastname: Stuart
mesh_terms: D000818:Animals; D002460:Cell Line; D007181:Inclusion Bodies, Viral / Q000737:chemistry* / Q000378:metabolism; D007304:Insect Viruses / Q000737:chemistry* / Q000502:physiology; D045586:Intranuclear Inclusion Bodies / Q000737:chemistry* / Q000378:metabolism; D009036:Moths / Q000737:chemistry / Q000821:virology; D033362:Powder Diffraction / Q000379:methods; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D015678:Viral Structural Proteins