Cala, Ali R <br/><br/>
The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 Å resolution.  [electronic resource] 

 -  Acta crystallographica. Section F, Structural biology communications  12 2016 
 - 885-891 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>2053-230X 
<br/><br/><label>Standard No.: </label>10.1107/S2053230X16018525  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Bacterial Proteins--chemistry<br/>Bartonella henselae--chemistry<br/>Binding Sites<br/>Cloning, Molecular<br/>Crystallography, X-Ray<br/>Dihydrodipicolinate Reductase--chemistry<br/>Escherichia coli--genetics<br/>Gene Expression<br/>Models, Molecular<br/>NADP--chemistry<br/>Plasmids--chemistry<br/>Protein Binding<br/>Protein Conformation, alpha-Helical<br/>Protein Conformation, beta-Strand<br/>Protein Interaction Domains and Motifs<br/>Protein Multimerization<br/>Recombinant Proteins--chemistry<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity