title: Crystallization of Sindbis virus and its nucleocapsid.
abstract: Crystals of Sindbis virus, which contains a lipid-bilayer membrane, have been grown using polyethylene glycol. The space group is R32, a = b = 640 A, c = 1520 A. The crystals are highly mosaic, and recorded diffraction is therefore restricted to spacings of about 30 A. The crystals show that the packing of glycoproteins E1 and E2 in the icosahedral outer shell is sufficiently precise that it permits regular and repeated interactions between virus particles in the lattice. Crystals of Sindbis nucleocapsids have also been grown. The limited diffraction data are consistent with close packing of nucleocapsids 404 A in diameter.
authors.affiliation: Howard Hughes Medical Institute, Harvard University, Cambridge, MA 02138-2092.
authors.forename: S C
authors.initials: SC
authors.lastname: Harrison
authors.forename: R K
authors.initials: RK
authors.lastname: Strong
authors.forename: S
authors.initials: S
authors.lastname: Schlesinger
authors.forename: M J
authors.initials: MJ
authors.lastname: Schlesinger
mesh_terms: D002213:Capsid / Q000737:chemistry*; D003460:Crystallization; D008562:Membrane Glycoproteins / Q000737:chemistry*; D011092:Polyethylene Glycols; D012845:Sindbis Virus / Q000737:chemistry*; D014759:Viral Envelope Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins; C022012:glycoprotein E1, Sindbis virus; C064950:glycoprotein E2, Sindbis virus; D011092:Polyethylene Glycols