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Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae

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  • San Hadǽi
  • Abel Garcia-Pino
  • Sergio Martinez-Rodriguez
  • Koen Verschueren
  • Mikkel Christensen-Dalsgaard
  • Kenn Gerdes
  • Jurij Lah
  • Remy Loris
The genome of Vibrio cholerae encodes two higBA toxin-antitoxin (TA) modules that are activated by amino-acid starvation. Here, the TA complex of the second module, higBA2, as well as the C-terminal domain of the corresponding HigA2 antitoxin, have been purified and crystallized. The HigBA2 complex crystallized in two crystal forms. Crystals of form I belonged to space group P21212, with unit-cell parameters a = 129.0, b = 119.8, c = 33.4 Å, and diffracted to 3.0 Å resolution. The asymmetric unit is likely to contain a single complex consisting of two toxin monomers and one antitoxin dimer. The second crystal form crystallized in space group P3221, with unit-cell parameters a = 134.5, c = 55.4 Å. These crystals diffracted to 2.2 Å resolution and probably contain a complex with a different stoichiometry. Crystals of the C-terminal domain of HigA2 belonged to space group C2, with unit-cell parameters a = 115.4, b = 61.2, c = 73.8 Å, β = 106.7°, and diffracted to 1.8 Å resolution.
OriginalsprogEngelsk
TidsskriftActa Crystallographica. Section F: Structural Biology and Crystallization Communications Online
Vol/bind69
Udgave nummerPt 9
Sider (fra-til)1052-9
Antal sider8
ISSN1744-3091
DOI
StatusUdgivet - sep. 2013

ID: 49868581