Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli.
The Escherichia coli thioesterase I specifically catalyzes the deacylation of fatty acyl-CoA thioesters, especially those with long acyl groups (C(12)-C(18)). Single crystals of thioesterase I (E.C. 3. 1.2.2) from E. coli have been obtained using methoxypolyethylene glycol 5000 (PEG-MME 5K) as a precipitant at room temperature in 21 d. The crystals belong to the tetragonal space group P4(1)2(1)2 or its enantiomorph P4(3)2(1)2, with unit-cell parameters a = b = 50.85 (7), c = 171.5 (1) A. The crystals diffract to beyond 2.4 A resolution. There is one molecule of molecular weight 20.5 kDa in the asymmetric unit, with a solvent content of 55%.
Lo
Y C
YC
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Lee
Y L
YL
Shaw
J F
JF
Liaw
Y C
YC
D020816:Amino Acid Motifs; D016384:Consensus Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D008066:Lipolysis; D010170:Palmitoyl-CoA Hydrolase / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012984:Software
D010170:Palmitoyl-CoA Hydrolase