The Escherichia coli thioesterase I specifically catalyzes the deacylation of fatty acyl-CoA thioesters, especially those with long acyl groups (C12-C18). Single crystals of thioesterase I (E.C. 188.8.131.52) 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 P41212 or its enantiomorph P43212, with unit-cell parameters a = b = 50.85 (7), c = 171.5 (1) Å. The crystals diffract to beyond 2.4 Å resolution. There is one molecule of molecular weight 20.5 kDa in the asymmetric unit, with a solvent content of 55%.
|Number of pages||2|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - 2000 Jul 3|
All Science Journal Classification (ASJC) codes
- Structural Biology