Open AccessPurification and crystallization of Phd, the antitoxin of the phd / doc operon
Author(s) -
GarciaPino Abel,
Sterckx Yann,
Vandenbussche Guy,
Loris Remy
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109051550
Subject(s) - crystallization , operon , antitoxin , resolution (logic) , crystallography , bacteriophage , chemistry , biophysics , biology , biochemistry , toxin , organic chemistry , gene , escherichia coli , computer science , artificial intelligence
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 Å resolution. Crystals of untagged Phd purified from the Phd–Doc complex diffract to 2.25 Å resolution. These crystals are partially merohedrally twinned and contain the full‐length version of the protein.