EC Number   |
|---|
   2.8.3.16 | beta-aspartyl-CoA thioester intermediate is identified by x-ray crystallography |
| 2.8.3.16 | crystallization and structure determination of the enzyme/oxalyl-CoA complex, hanging drop technique. Crystallization and structure determination of the D169A, D169E, and D169S mutants |
| 2.8.3.16 | FRC variants W48F and W48Q, hanging drop vapour diffusion method |
| 2.8.3.16 | His6-tagged enzyme, in complex with CoA, hanging drop vapor diffusion method, using 24% (w/v) PEG 4000 and 100 mM bicine, pH 8.8 |
| 2.8.3.16 | purified recombinant enzyme from overexpression in Escherichia coli, hanging drop method, protein solution: 7.5 mg/ml, 25 mM MES, pH 6.2, 10% glycerol, drop volume 0.002 ml, reservoir solution: 100 mM HEPES, pH 7.5, 26% polyethylene glycol 4000, 0.5 M MgCl2, 291 K, 1 week, X-ray diffraction structure determination and analysis |
| 2.8.3.16 | purified recombinant selenocysteine-substituted enzyme, hanging drop method, protein solution: 4.75 mg/ml, 25 mM MES, pH 6.2, 10% glycerol, drop volume 0.002 ml, reservoir solution: 100 mM HEPES, pH 7.5, 26% polyethylene glycol 4000, 0.5 M MgCl2, 291 K, 2 weeks, X-ray diffraction structure determination and analysis |
