Published in
International Union of Crystallography, Acta Crystallographica Section D: Biological Crystallography, 11(55), p. 1952-1954, 1999
DOI: 10.1107/s0907444999011361
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Crystallization and preliminary X-ray diffraction analysis of the homodimeric form α2 of the HU protein from Escherichia coli
,
Nadège Hervouet,
Jacques Oberto,
Charles Zelwer,
Bertrand Castaing
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Abstract
The homodimeric form α2 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 Å, and contain one monomer per asymmetric unit. A full diffraction data set was collected to 2.3 Å 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.