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Crystallization and preliminary X-ray diffraction studies of the enoyl-ACP reductase from Escherichia coli
U G Wagner1, H Bergler, S Fuchsbichler
1Institut für Physikalische Chemie, Karl-Franzens-Universität Graz, Austria.
Journal of Molecular Biology
|October 14, 1994
Abstract:
A crystal of the FabI protein from Escherichia coli has been obtained from polyethylene glycol (M(r) = 400) solution with sodium citrate at pH 8.5, by the hanging-drop technique at 4 degrees C. The crystal belongs to the hexagonal space group P6(1)22 (or P6(5)22) with cell dimensions of a = b = 81.1 A and c = 331.5 A. There are two molecules in the asymmetric unit and the crystal diffracts to 2.5 A resolution.