Crystallization and preliminary X-ray analysis of beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli.
Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase, a key enzyme for the biosynthesis of unsaturated fatty acids in E. coli, has been crystallized by the vapor diffusion method at pH 5.0-5.5 using 20% (w/v) polyethylene glycol (molecular weight 8000) as a precipitant. Two crystal forms have been characterized, and both diffract to at least 1.6 A. The orthorhombic crystals belong to space group P2(1)2(1)2(1), with cell constants of a = 68.4 A, b = 87.3 A, and c = 60.3 A. Monoclinic crystals are of space group C2, with a = 131.9 A, b = 71.5 A, c = 92.5 A, and beta = 103.5 degrees.
Sharma
A
A
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.
Henderson
B S
BS
Schwab
J M
JM
Smith
J L
JL
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D054889:Fatty Acid Synthase, Type II; D006836:Hydro-Lyases / Q000302:isolation & purification*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D006836:Hydro-Lyases; C047118:3-hydroxyacyl-(acyl-carrier-protein) dehydratase; D054889:Fatty Acid Synthase, Type II