Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli

Yu Chih Lo, Ya Lin Lee, Jei Fu Shaw, Yen Chywan Liaw

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

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. 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 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%.

Original languageEnglish
Pages (from-to)756-757
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number6
DOIs
Publication statusPublished - 2000 Jul 3

All Science Journal Classification (ASJC) codes

  • Structural Biology

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