Publikation: Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli
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2004
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Acta crystallographica Section D : Biological Crystallography. 2004, 60(Pt 3), pp. 531-533. ISSN 0907-4449. eISSN 1399-0047. Available under: doi: 10.1107/S0907444903028713
Zusammenfassung
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.
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570 Biowissenschaften, Biologie
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GERBER, Kinga, André SCHIEFNER, Peter SEIGE, Kay DIEDERICHS, Winfried BOOS, Wolfram WELTE, 2004. Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli. In: Acta crystallographica Section D : Biological Crystallography. 2004, 60(Pt 3), pp. 531-533. ISSN 0907-4449. eISSN 1399-0047. Available under: doi: 10.1107/S0907444903028713BibTex
@article{Gerber2004Cryst-40701, year={2004}, doi={10.1107/S0907444903028713}, title={Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli}, number={Pt 3}, volume={60}, issn={0907-4449}, journal={Acta crystallographica Section D : Biological Crystallography}, pages={531--533}, author={Gerber, Kinga and Schiefner, André and Seige, Peter and Diederichs, Kay and Boos, Winfried and Welte, Wolfram} }
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