Crystallization and preliminary X-ray diffraction analysis of bacteriophage varphi12 packaging factor P7

Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2368-70. doi: 10.1107/S0907444904026952. Epub 2004 Nov 26.

Abstract

Bacteriophage varphi12 protein P7 is a structural component of the polymerase complex and ensures stable packaging of the genomic RNA. varphi12 P7 has been cloned, purified and crystallized. Crystals belong to space group P3(2)21, with unit-cell parameters a = 75.7, b = 75.7, c = 45.2 A, alpha = 90, beta = 90, gamma = 120 degrees , and diffract beyond 2.0 A. Multiple anomalous dispersion data have been collected from crystals of selenomethionylated P7. Mass spectroscopy showed proteolysis of the crystallized protein and a truncated form, P7DeltaC, gave crystals of similar morphology. Cross-linking experiments implicated the N-terminal domain of P7 as being essential for dimerization.

Publication types

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

MeSH terms

  • Bacteriophages / metabolism*
  • Chromatography, Gel
  • Cloning, Molecular
  • Cross-Linking Reagents / pharmacology
  • Crystallization
  • Crystallography, X-Ray
  • Dimerization
  • Glycoside Hydrolases / chemistry*
  • Mass Spectrometry
  • Protein Structure, Tertiary
  • RNA / chemistry
  • Selenomethionine / chemistry
  • Time Factors
  • Viral Nonstructural Proteins / chemistry*
  • X-Ray Diffraction

Substances

  • Cross-Linking Reagents
  • Viral Nonstructural Proteins
  • RNA
  • Selenomethionine
  • Glycoside Hydrolases
  • P7 protein, bacteriophage PRD1