PMID:10818355
| Citation |
Lo, YC, Lee, YL, Shaw, JF and Liaw, YC (2000) Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 56:756-7 |
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| Abstract |
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%. |
| Links | |
| Keywords |
Amino Acid Motifs; Consensus Sequence; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/metabolism; Lipolysis; Palmitoyl-CoA Hydrolase/chemistry; Palmitoyl-CoA Hydrolase/metabolism; Sequence Homology, Amino Acid; Software |
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