PMID:15213392
| Citation |
Koedding, J, Polzer, P, Killig, F, Howard, SP, Gerber, K, Seige, P, Diederichs, K and Welte, W (2004) Crystallization and preliminary X-ray analysis of a C-terminal TonB fragment from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 60:1281-3 |
|---|---|
| Abstract |
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 P2(1) 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. |
| Links |
PubMed Online version:10.1107/S0907444904009722 |
| Keywords |
Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Membrane Proteins/chemistry; Peptide Fragments/chemistry |
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