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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1571-6. doi: 10.1107/S1744309112045563. Epub 2012 Nov 28.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Capsid Proteins / chemistry
  • Crystallization
  • Crystallography, X-Ray
  • H-1 parvovirus / chemistry*
  • H-1 parvovirus / isolation & purification
  • X-Ray Diffraction

Substances

  • Capsid Proteins