PMID:10531506
| Citation |
Coste, F, Hervouet, N, Oberto, J, Zelwer, C and Castaing, B (1999) Crystallization and preliminary X-ray diffraction analysis of the homodimeric form alpha2 of the HU protein from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 55:1952-4 |
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| 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. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Crystallization; DNA-Binding Proteins/chemistry; Dimerization; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Geobacillus stearothermophilus; X-Ray Diffraction |
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