Accueil > Publications > Recherche par années > Années 1990 > 1999

Coste, F ; Hervouet, N ; Oberto, J ; Zelwer, C ; Castaing, B

Crystallization and preliminary X-ray diffraction analysis of the homodimeric form a(2) of the HU protein from Escherichia coli

Acta Crystallographica Section D-Biological Crystallography 55 1952-1954 Part 11

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Abstract :

The homodimeric form a(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 Angstrom, and contain one monomer per asymmetric unit. A full diffraction data set was collected to 2.3 Angstrom 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.