EC Number   |
|---|
    5.3.1.1 | - |
| 5.3.1.1 | comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms |
| 5.3.1.1 | crystal structure analysis |
| 5.3.1.1 | crystal structure analysis, overview |
| 5.3.1.1 | crystal structure of PfTIMat 2.2 A resolution or 2.8 A resolution, crystal structure of the enzyme in complex with phosphoglycolate at 1.9 A resolution, crystal structure of the enzyme in complex with glycerol phosphate at 2.4 A resolution, crystal structure of the enzyme in complex with 2-phosphoglycerate at 1.1 A resolution or 2.4 A resolution |
| 5.3.1.1 | crystal structure of the recombinant enzyme complexed with phosphoglycolohydroxamate, at 1.8 A resolution |
| 5.3.1.1 | crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution |
| 5.3.1.1 | crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex, at 2.7 A resolution |
| 5.3.1.1 | crystals are grown at 18°C from hanging drops by mixing 0.005 ml of the enzyme, 5 mg/ml, with 0.005 ml of the reservoir solution, 28% w/v PEG 1500 and 0.001 ml of 30% v/v 1,6-hexanediol |
| 5.3.1.1 | determination by molecular replacement, at 2.3 A resolution and in the closed state. Phosphate acts as a competitive inhibitor and occupies the binding pocket. Binding pocket has a very stable conformation even without a substrate |
