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

Natalie De Jonge, Lieven Buts, Joris Vangelooven, Laurence Van Melderen, Lode Wyns, Remy Loris

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

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 (CcdBVfi) 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 unitcell parameters a = 58.5, b = 43.6, c = 37.5 A, beta = 110.0°, and diffracts to 1.7 A resolution. The complex of CcdBVfi with the GyrA14Vfi 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 GyrA14Ec crystallizes in space group C2, with unit-cell parameters a = 130.1, b = 90.8, c = 58.1 A, beta = 102.6°, and diffracts to 1.95 A. Finally, a complex between CcdBVfi and part of the F-plasmid antitoxin CcdAF 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.
Original languageEnglish
Pages (from-to)356-360
Number of pages5
JournalActa Crystallogr F Struct Biol Commun
Volume63
Publication statusPublished - 2007

Keywords

  • TA module
  • toxin-antitoxin
  • crystallography
  • gyrase
  • structural biology

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