EC Number   |
|---|
    2.3.3.16 | comparison of rigidity in citrate synthases from thermophiles to investgate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein |
| 2.3.3.16 | comparison of rigidity in citrate synthases from thermophiles to investigate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein |
| 2.3.3.16 | crystal structure analysis of chimeric mutants with exchange of large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus |
| 2.3.3.16 | crystal structure at 1.7 A resolution. Like other Type-I CS, citrate synthase functions as a dimer and each monomer consists of a large domain and a small domain. The oxaloacetate binding site locates at the cleft between the two domains, and the active site is more closed upon binding of the oxaloacetate substrate than binding of the citrate product |
| 2.3.3.16 | hanging drop vapor diffusion method, using 0.1 M CHES pH 9.5, 12% (w/v) PEG 4000, 1 mM oxaloacetate |
| 2.3.3.16 | hanging drop vapor diffusion method, using 0.2 M magnesium chloride hexahydrate, 0.1M Tris pH 8.5, 3.4 M 1,6-hexandiol |
| 2.3.3.16 | hanging drop vapour diffusion method, from 2-2.3 M ammonium sulfate, 2% v/v polyethylene glycol 400, 0.1 M HEPS, pH 6.0, X-ray diffraction analysis, structure determination and modeling: 3 identical dimer units arranged about a central 3-fold axis |
| 2.3.3.16 | hanging drop vapour diffusion method, room temperature, 2 mg/ml protein concentration, precipitation by 0.1 M sodium citrate and 0.1 M ammonium phosphate, 20 mM Tris-HCl, pH 8.0, 25 mM KCl, x-ray structure analysis, structural basis of high thermostability |
| 2.3.3.16 | hanging-drop vapour diffusion method, 2.7 A resolution |
| 2.3.3.16 | hanging-drop vapour-diffusion method from 2.0-2.2 M ammonium sulfate, 2% PEG 400, and 0.1 M Na-HEPES at pH 6.0. the NADH-bound form of mutant R109L is obtained by soaking a variant crystal in a solution containing 1.22 mM NADH, 2.8 M ammonium sulfate, 2% polyethylene glycol 400 and 0.1 M Na-Hepes at pH 6.0 |
