Crystallization and preliminary X-ray diffraction analysis of the homodimeric form alpha2 of the HU protein from Escherichia coli.
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.
Coste
F
F
Centre de Biophysique Moléculaire, Rue Charles Sadron, 45071 Orleans CEDEX 2, France.
Hervouet
N
N
Oberto
J
J
Zelwer
C
C
Castaing
B
B
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D004268:DNA-Binding Proteins / Q000737:chemistry*; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D001411:Geobacillus stearothermophilus; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C040330:histone-like protein HU, bacteria