Gayathri, P <br/><br/>
Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site.  [electronic resource] 

 -  Acta crystallographica. Section D, Biological crystallography  Aug 2009 
 - 847-57 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1399-0047 
<br/><br/><label>Standard No.: </label>10.1107/S0907444909018666  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Catalytic Domain<br/>Crystallization<br/>Crystallography, X-Ray<br/>Dimerization<br/>Ligands<br/>Mutant Proteins--chemistry<br/>Phenylalanine--metabolism<br/>Plasmodium falciparum--enzymology<br/>Protein Binding<br/>Protein Conformation<br/>Protein Interaction Domains and Motifs<br/>Protozoan Proteins--chemistry<br/>Triose-Phosphate Isomerase--chemistry<br/>Water