EC Number   |
Reference |
|---|
    2.3.1.16 | - |
486418, 486431, 486433 |
| 2.3.1.16 | modeling of the heterotetrameric alpha2beta2 complex |
757515 |
| 2.3.1.16 | purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml of protein solution is mixed with 0.002 ml reservoir solution containing 0.1 M TrisHCl, pH 8.5, 300 mM MgCl2, and 25% w/v polyethylene glycol 4000, X-ray diffraction structure determination and analysis at 2.1-2.4 A resolution |
675383 |
| 2.3.1.16 | purified recombinant wild-type and mutant enzymes in apoform and in complex with CoA, hanging drop vapour diffusion method, mixing of 0.002 ml of 4.4 mg/ml protein in 25 mM Tris-HCl pH 8.0, 1 mM DTT, with 0.002 ml of reservoir solution containing 100 mM MES, pH 6.6, or MOPS, pH 7.2, and 14-15% PEG MME 5000, equilibration against 1 ml of reservoir solution, 22°C, method optimization, X-ray diffraction structure determination and analysis at 2.0-3.3 A resolution, modeling |
735368 |
| 2.3.1.16 | to 1.5 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state |
719874 |
| 2.3.1.16 | to 1.8 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state |
719874 |
