title: Production, purification, crystallization and structure determination of H-1 Parvovirus.
abstract: Crystals of H-1 Parvovirus (H-1PV), an antitumor gene-delivery vector, were obtained for DNA-containing capsids and diffracted X-rays to 2.7 Å resolution using synchrotron radiation. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a=255.4, b=350.4, c=271.6 Å, β=90.34°. The unit cell contained two capsids, with one capsid per crystallographic asymmetric unit. The H-1PV structure has been determined by molecular replacement and is currently being refined.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA.
authors.forename: Sujata
authors.initials: S
authors.lastname: Halder
authors.forename: Hyun Joo
authors.initials: HJ
authors.lastname: Nam
authors.forename: Lakshmanan
authors.initials: L
authors.lastname: Govindasamy
authors.forename: Michèle
authors.initials: M
authors.lastname: Vogel
authors.forename: Christiane
authors.initials: C
authors.lastname: Dinsart
authors.forename: Nathalie
authors.initials: N
authors.lastname: Salomé
authors.forename: Robert
authors.initials: R
authors.lastname: McKenna
authors.forename: Mavis
authors.initials: M
authors.lastname: Agbandje-McKenna
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D052661:H-1 parvovirus / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D036022:Capsid Proteins