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

TitlePurification and crystallization of Phd, the antitoxin of the phd/doc operon.
Publication TypeJournal Article
Year of Publication2010
AuthorsGarcia-Pino, A., Y. Sterckx, G. Vandenbussche, and R. Loris
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume66
IssuePt 2
Pagination167-71
Date Published2010 Feb 1
Type of Articleta
ISSN1744-3091
KeywordsAntitoxins, Bacteriophage P1, Mass Spectrometry, Operon, Viral Proteins, X-Ray Diffraction
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.

DOI10.1107/S1744309109051550
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID20124714
PubMed Central IDPMC2815684