PMID:10818351

Citation	Janson, CA, Konstantinidis, AK, Lonsdale, JT and Qiu, X (2000) Crystallization of Escherichia coli beta-ketoacyl-ACP synthase III and the use of a dry flash-cooling technique for data collection. Acta Crystallogr. D Biol. Crystallogr. 56:747-8
Abstract	beta-Ketoacyl-acyl carrier protein (ACP) synthase III (FabH) is a condensing enzyme active in the fatty-acid biosynthesis pathway of bacteria. The enzymes of this pathway provide a set of targets for the discovery of previously unknown antibiotics. FabH from Escherichia coli has been crystallized in two crystal forms using the sitting-drop vapor-diffusion technique. The first form crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 63.1, b = 65.1, c = 166.5 A; the second form crystallized in the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 72.7, c = 99.8 A. A flash-cooling technique using no cryoprotectant was utilized in obtaining data from the second type of crystals.
Links	PubMed
Keywords	3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/chemistry; Bacterial Proteins/chemistry; Crystallization; Data Interpretation, Statistical; Escherichia coli/enzymology; Freezing; X-Ray Diffraction/methods
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