Purification and crystallization of Vibrio fischeri CcdB and its complexes with fragments of gyrase and CcdA.

TitlePurification and crystallization of Vibrio fischeri CcdB and its complexes with fragments of gyrase and CcdA.
Publication TypeJournal Article
Year of Publication2007
AuthorsDe Jonge, N., L. Buts, J. Vangelooven, N. Mine, L. Van Melderen, L. Wyns, and R. Loris
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume63
IssuePt 4
Pagination356-60
Date Published2007 Apr 1
Type of Articleta
ISSN1744-3091
KeywordsAliivibrio fischeri, Amino Acid Sequence, Bacterial Proteins, Base Sequence, Crystallization, DNA Gyrase, DNA Primers, Molecular Sequence Data, Protein Conformation
Abstract

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 I23 or I2(1)3, with unit-cell parameter a = 84.5 A, and diffracts to 1.5 A resolution. The second crystal form belongs to space group C2, with unit-cell parameters a = 58.5, b = 43.6, c = 37.5 A, beta = 110.0 degrees, and diffracts to 1.7 A resolution. The complex of CcdB(Vfi) with the GyrA14(Vfi) fragment of V. fischeri gyrase crystallizes in space group P2(1)2(1)2(1), with unit-cell parameters a = 53.5, b = 94.6, c = 58.1 A, and diffracts to 2.2 A resolution. The corresponding mixed complex with E. coli GyrA14(Ec) crystallizes in space group C2, with unit-cell parameters a = 130.1, b = 90.8, c = 58.1 A, beta = 102.6 degrees, and diffracts to 1.95 A. Finally, a complex between CcdB(Vfi) and part of the F-plasmid antitoxin CcdA(F) crystallizes in space group P2(1)2(1)2(1), with unit-cell parameters a = 46.9, b = 62.6, c = 82.0 A, and diffracts to 1.9 A resolution.

DOI10.1107/S1744309107012092
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID17401216
PubMed Central IDPMC2330220