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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, ?=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.

SUBMITTER: Halder S

PROVIDER: S-EPMC3509992 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Production, purification, crystallization and structure determination of H-1 Parvovirus.

Halder Sujata S Nam Hyun Joo HJ Govindasamy Lakshmanan L Vogel Michèle M Dinsart Christiane C Salomé Nathalie N McKenna Robert R Agbandje-McKenna Mavis M

Acta crystallographica. Section F, Structural biology and crystallization communications 20121128 Pt 12

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. ...[more]

PMID: 23192051

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