Publikation:

Crystallization and preliminary X-ray analysis of a C-terminal TonB fragment from Escherichia coli

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Crystallization_and_preliminary.pdf
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2004

Autor:innen

Koedding, Jiri
Polzer, Patrick
Killig, Frank
Howard, S. Peter

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http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-40641
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https://doi.org/10.1107/S0907444904009722
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Attribution-NonCommercial-NoDerivs 2.0 Generic

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Acta Crystallographica, Section D. 2004, 60(7), pp. 1281-1283. ISSN 0907-4449. Available under: doi: 10.1107/S0907444904009722

Zusammenfassung

The TonB protein located in the cell wall of Gram-negative bacteria mediates the proton motive force from the cytoplasmic membrane to specific outer membrane transporters. A C-terminal fragment of TonB from Escherichia coli consisting of amino-acid residues 147-239 (TonB-92) has been purified and crystallized. Crystals grew in space group P21 to dimensions of about 1.0 x 0.12 x 0.12 mm. A native data set has been obtained to 1.09 A resolution.

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570 Biowissenschaften, Biologie

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ISO 690KOEDDING, Jiri, Patrick POLZER, Frank KILLIG, S. Peter HOWARD, Kinga GERBER, Peter SEIGE, Kay DIEDERICHS, Wolfram WELTE, 2004. Crystallization and preliminary X-ray analysis of a C-terminal TonB fragment from Escherichia coli. In: Acta Crystallographica, Section D. 2004, 60(7), pp. 1281-1283. ISSN 0907-4449. Available under: doi: 10.1107/S0907444904009722
BibTex
@article{Koedding2004Cryst-7191,
  year={2004},
  doi={10.1107/S0907444904009722},
  title={Crystallization and preliminary X-ray analysis of a C-terminal TonB fragment from Escherichia coli},
  number={7},
  volume={60},
  issn={0907-4449},
  journal={Acta Crystallographica, Section D},
  pages={1281--1283},
  author={Koedding, Jiri and Polzer, Patrick and Killig, Frank and Howard, S. Peter and Gerber, Kinga and Seige, Peter and Diederichs, Kay and Welte, Wolfram}
}
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