Purification and crystallization of Phd, the antitoxin of the phd/doc operon

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):167-71. doi: 10.1107/S1744309109051550. Epub 2010 Jan 27.

Abstract

The antitoxin Phd from the phd/doc module of bacteriophage P1 was crystallized in two distinct crystal forms. Crystals of His-tagged Phd contain a C-terminally truncated version of the protein and diffract to 2.20 A resolution. Crystals of untagged Phd purified from the Phd-Doc complex diffract to 2.25 A resolution. These crystals are partially merohedrally twinned and contain the full-length version of the protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antitoxins / chemistry*
  • Antitoxins / genetics
  • Antitoxins / isolation & purification*
  • Bacteriophage P1 / chemistry*
  • Bacteriophage P1 / genetics
  • Mass Spectrometry
  • Operon*
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics
  • Viral Proteins / isolation & purification*
  • X-Ray Diffraction

Substances

  • Antitoxins
  • Viral Proteins