Chin, Ko-Hsin <br/><br/>
Crystal structure of a putative acyl-CoA thioesterase from Xanthomonas campestris (XC229) adopts a tetrameric hotdog fold of epsilongamma mode.  [electronic resource] 

 -  Proteins  Aug 2006 
 - 823-6 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1097-0134 
<br/><br/><label>Standard No.: </label>10.1002/prot.21037  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Bacterial Proteins--chemistry<br/>Binding Sites--genetics<br/>Crystallization<br/>Crystallography, X-Ray--methods<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Palmitoyl-CoA Hydrolase--chemistry<br/>Protein Structure, Secondary<br/>Protein Structure, Tertiary<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity<br/>Xanthomonas campestris--genetics