Open AccessPurification and crystallization of Vibrio fischeri CcdB and its complexes with fragments of gyrase and CcdA
Author(s) -
Buts Lieven,
De Jonge Natalie,
Mine Natacha,
Wyns Lode,
Loris Remy,
Vangelooven Joris,
Van Melderen Laurence
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107012092
Subject(s) - crystallography , physics , dna gyrase , resolution (logic) , escherichia coli , crystallization , plasmid , stereochemistry , chemistry , dna , biochemistry , artificial intelligence , computer science , gene , thermodynamics
The ccd toxin–antitoxin module from the Escherichia coli F plasmid has a homologue on the Vibrio fischeri integron. The homologue of the toxin (CcdB Vfi ) was crystallized in two different crystal forms. The first form belongs to space group I 23 or I 2 1 3, with unit‐cell parameter a = 84.5 Å, and diffracts to 1.5 Å resolution. The second crystal form belongs to space group C 2, with unit‐cell parameters a = 58.5, b = 43.6, c = 37.5 Å, β = 110.0°, and diffracts to 1.7 Å resolution. The complex of CcdB Vfi with the GyrA14 Vfi fragment of V. fischeri gyrase crystallizes in space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 53.5, b = 94.6, c = 58.1 Å, and diffracts to 2.2 Å resolution. The corresponding mixed complex with E. coli GyrA14 Ec crystallizes in space group C 2, with unit‐cell parameters a = 130.1, b = 90.8, c = 58.1 Å, β = 102.6°, and diffracts to 1.95 Å. Finally, a complex between CcdB Vfi and part of the F‐plasmid antitoxin CcdA F crystallizes in space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 46.9, b = 62.6, c = 82.0 Å, and diffracts to 1.9 Å resolution.