Crystallization of Escherichia coli beta-ketoacyl-ACP synthase III and the use of a dry flash-cooling technique for data collection.
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.
Janson
C A
CA
Department of Structural Biology, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406, USA. cheryl_a_janson@sbphrd.com
Konstantinidis
A K
AK
Lonsdale
J T
JT
Qiu
X
X
D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D003627:Data Interpretation, Statistical; D004926:Escherichia coli / Q000201:enzymology*; D005615:Freezing; D014961:X-Ray Diffraction / Q000379:methods
D001426:Bacterial Proteins; C077402:3-ketoacyl-acyl carrier protein synthase III; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase