Crystallization and preliminary X-ray diffraction analysis of the homodimeric form alpha2 of the HU protein from Escherichia coli.

Abstract : The homodimeric form alpha(2) of the Escherichia coli DNA-binding protein HU was crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The crystals belong to space group I222, with unit-cell parameters a = 31.09, b = 55.34, c = 117. 63 A, and contain one monomer per asymmetric unit. A full diffraction data set was collected to 2.3 A resolution on a conventional X-ray source. The molecular-replacement method, using the HU crystallographic model from Bacillus stearothermophilus as a starting point, gave a reliable solution for the rotation and translation functions.
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Submitted on : Monday, May 13, 2019 - 3:59:43 PM
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  • HAL Id : hal-02127644, version 1
  • PUBMED : 10531506

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Franck Coste, N. Hervouet, J. Oberto, C. Zelwer, Bertrand Castaing. Crystallization and preliminary X-ray diffraction analysis of the homodimeric form alpha2 of the HU protein from Escherichia coli.. Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 1999, 55 (Pt 11), pp.1952-4. ⟨hal-02127644⟩

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