title: Crystallization of the major coat protein of PRD1, a bacteriophage with an internal membrane.
abstract: The major multimeric coat protein, P3, of the bacterial virus PRD1 has been crystallized by vapor diffusion from polyethylene glycol 4000. The PRD1-P3 crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 121.6 A, b = 123.2 A, c = 128.6 A and diffract to 3.0 A resolution. Density measurements show that there is one trimer (3 x 43.1 kDa) per asymmetric unit and a high solvent content of 67%. A self-rotation function calculation shows a pronounced peak indicating a non-crystallographic threefold axis. This indicates that the major viral capsomer is a trimer and allows the viral T-number to be postulated.
authors.affiliation: Wistar Institute, Philadelphia, PA 19104.
authors.forename: P L
authors.initials: PL
authors.lastname: Stewart
authors.forename: S
authors.initials: S
authors.lastname: Ghosh
authors.forename: D H
authors.initials: DH
authors.lastname: Bamford
authors.forename: R M
authors.initials: RM
authors.lastname: Burnett
mesh_terms: D001435:Bacteriophages / Q000648:ultrastructure*; D002213:Capsid / Q000737:chemistry*; D003461:Crystallography; D008563:Membrane Lipids / Q000737:chemistry; D008854:Microscopy, Electron; D014961:X-Ray Diffraction
chemical_list: D008563:Membrane Lipids