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  • Title: Crystallization and preliminary X-ray diffraction analysis of the homodimeric form alpha2 of the HU protein from Escherichia coli.
    Author: Coste F, Hervouet N, Oberto J, Zelwer C, Castaing B.
    Journal: Acta Crystallogr D Biol Crystallogr; 1999 Nov; 55(Pt 11):1952-4. PubMed ID: 10531506.
    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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