PMID:14993683

Citation	Gerber, K, Schiefner, A, Seige, P, Diederichs, K, Boos, W and Welte, W (2004) Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 60:531-3
Abstract	Aes belongs to the family of hormone-sensitive lipases and has acetyl-esterase activity. It is also known to control maltose uptake through interaction with MalT, the central regulator of the Escherichia coli maltose system. Aes was crystallized as an N-terminally His(6)-tagged protein both in the native form and with selenomethionine substitution. Crystals grew in both cases in space group R32 to dimensions of about 0.2 x 0.15 x 0.05 mm (native His(6)-Aes) and about 0.5 x 0.3 x 0.1 mm (SeMet-His(6)-Aes). A native data set has been obtained at 2.4 A resolution; the selenomethionine-substituted Aes crystals diffracted to 3.0 A resolution.
Links	PubMed Online version:10.1107/S0907444903028713
Keywords	Acetylesterase/chemistry; Acetylesterase/genetics; Acetylesterase/metabolism; Crystallization; Crystallography, X-Ray; DNA-Binding Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Protein Binding; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Transcription Factors/metabolism
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