• Medientyp: E-Artikel
  • Titel: Crystallization and preliminary X-ray analyses of catabolite control protein A, free and in complex with its DNA-binding site
  • Beteiligte: Tebbe, Jan; Orth, Peter; Küster-Schöck, Elke; Hillen, Wolfgang; Saenger, Wolfram; Hinrichs, Winfried
  • Erschienen: International Union of Crystallography (IUCr), 2000
  • Erschienen in: Acta Crystallographica Section D Biological Crystallography, 56 (2000) 1, Seite 67-69
  • Sprache: Nicht zu entscheiden
  • DOI: 10.1107/s0907444999013104
  • ISSN: 0907-4449
  • Schlagwörter: General Medicine ; Structural Biology
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  • Beschreibung: The catabolite control protein (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR/LacI. CcpA with an N-terminal His-tag was used for crystallization. Crystals of free CcpA and of CcpA in complex with the putative operator sequence (catabolite responsive elements, CRE) were obtained by vapour-diffusion techniques at 291 K using the hanging-drop method. CcpA crystals grown in the presence of polyethylene glycol 8000 belong to the hexagonal space group P6122 or P6522, with unit-cell parameters a = 74.4, c = 238.8 Å. These crystals diffract X-rays to 2.55 Å resolution and contain one monomer of the homodimeric protein per asymmetric unit. Crystals of the CcpA–CRE complex were obtained with ammonium sulfate as precipitant and belong to the tetragonal space group I4122, with unit-cell parameters a = 125, c = 400 Å and one complex per asymmetric unit. Although these co-crystals grew to a sufficient size, X-ray diffraction was limited to 8 Å resolution.