Publication
Title
Purification and crystallization of Phd, the antitoxin of the phd/doc operon
Author
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 angstrom resolution. Crystals of untagged Phd purified from the Phd-Doc complex diffract to 2.25 angstrom resolution. These crystals are partially merohedrally twinned and contain the full-length version of the protein.
Language
English
Source (journal)
Acta crystallographica: section F: structural biology and crystallization communications. - Copenhagen
COMMUNICATIONS
Publication
Copenhagen : 2010
ISSN
1744-3091
DOI
10.1107/S1744309109051550
Volume/pages
66 :2 (2010) , p. 167-171
ISI
000274085600011
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Publication type
Subject
External links
Web of Science
Record
Identifier
Creation 04.10.2018
Last edited 16.02.2023
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