title: Crystallization and preliminary X-ray analysis of a C-terminal TonB fragment from Escherichia coli.
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.
authors.affiliation: Department of Biology, University of Konstanz, 78457 Konstanz, Germany. jiri.koedding@uni-konstanz.de
authors.forename: Jiri
authors.initials: J
authors.lastname: Koedding
authors.forename: Patrick
authors.initials: P
authors.lastname: Polzer
authors.forename: Frank
authors.initials: F
authors.lastname: Killig
authors.forename: S Peter
authors.initials: SP
authors.lastname: Howard
authors.forename: Kinga
authors.initials: K
authors.lastname: Gerber
authors.forename: Peter
authors.initials: P
authors.lastname: Seige
authors.forename: Kay
authors.initials: K
authors.lastname: Diederichs
authors.forename: Wolfram
authors.initials: W
authors.lastname: Welte
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D010446:Peptide Fragments; C489181:tonB protein, E coli