Hermann, Johannes <br/><br/>
Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways.  [electronic resource] 

 -  Acta crystallographica. Section F, Structural biology communications  Dec 2018 
 - 754-764 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>2053-230X 
<br/><br/><label>Standard No.: </label>10.1107/S2053230X18015273  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Alcohol Dehydrogenase--chemistry<br/>Amino Acid Sequence<br/>Binding Sites--physiology<br/>Crystallography, X-Ray--methods<br/>Hydrogen Bonding<br/>Levilactobacillus brevis--chemistry<br/>Neutron Diffraction--methods<br/>Protein Structure, Secondary<br/>Protein Structure, Tertiary