Ködding, Jiri <br/><br/>
Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments.  [electronic resource] 

 -  The Journal of biological chemistry  Jan 2005 
 - 3022-8 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M411155200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Biological Transport<br/>Biological Transport, Active<br/>Crystallography, X-Ray<br/>Cytoplasm--metabolism<br/>Dimerization<br/>Escherichia coli--metabolism<br/>Escherichia coli Proteins--chemistry<br/>Light<br/>Membrane Proteins--chemistry<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Protein Conformation<br/>Protein Structure, Secondary<br/>Protein Structure, Tertiary<br/>Scattering, Radiation<br/>Ultracentrifugation