Skálová, Tereza <br/><br/>
Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution.  [electronic resource] 

 -  Journal of molecular biology  Oct 2005 
 - 282-94 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1016/j.jmb.2005.08.028  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Arthrobacter--enzymology<br/>Bacterial Proteins--chemistry<br/>Binding Sites<br/>Cold Temperature<br/>Crystallography, X-Ray<br/>Humans<br/>Ions--chemistry<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Protein Structure, Quaternary<br/>Sequence Alignment<br/>Solvents--chemistry<br/>beta-Galactosidase--chemistry