title: Purification and crystallization of Phd, the antitoxin of the phd/doc operon.
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.
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussel, Belgium.
authors.forename: Abel
authors.initials: A
authors.lastname: Garcia-Pino
authors.forename: Yann
authors.initials: Y
authors.lastname: Sterckx
authors.forename: Guy
authors.initials: G
authors.lastname: Vandenbussche
authors.forename: Remy
authors.initials: R
authors.lastname: Loris
mesh_terms: D000992:Antitoxins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D017101:Bacteriophage P1 / Q000737:chemistry* / Q000235:genetics; D013058:Mass Spectrometry; D009876:Operon; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D014961:X-Ray Diffraction
chemical_list: D000992:Antitoxins; D014764:Viral Proteins