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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

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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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ISO 690GERBER, 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/S0907444903028713
BibTex
@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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