Crystallization and preliminary X-ray diffraction studies of the enoyl-ACP reductase from Escherichia coli.
作者信息
Wagner U G, Bergler H, Fuchsbichler S, Turnowsky F, Högenauer G, Kratky C
机构信息
Institut für Physikalische Chemie, Karl-Franzens-Universität Graz, Austria.
出版信息
J Mol Biol. 1994 Oct 14;243(1):126-7. doi: 10.1006/jmbi.1994.1636.
PMID:7932735
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.
摘要
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