Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli

Authors: Gerber, Kinga; Schiefner, André; Seige, Peter; Diederichs, Kay; Boos, Winfried; Welte, Wolfram

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 531-533(3)

Publisher: Blackwell Publishing

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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 His₆-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 × 0.15 × 0.05 mm (native His₆-Aes) and about 0.5 × 0.3 × 0.1 mm (SeMet-His₆-Aes). A native data set has been obtained at 2.4 Å resolution; the selenomethionine-substituted Aes crystals diffracted to 3.0 Å resolution.

Keywords: esterase; Aes; acetyl-esterase

Document Type: Research article

DOI: 10.1107/S0907444903028713

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