EC Number   |
Reference |
|---|
   7.2.2.9 | crystallization and structure determination of the the apo- and phosphate-bound ATP-binding domain, hanging drop vapour diffusion method |
719129 |
| 7.2.2.9 | crystallization trials are performed at 18 °C by vapor diffusion using the hanging-drop technique, crystal structure of the catalytic fragment of a Sulfolobus solfataricus P-type ATPase, CopB-B, is determined with a 2.6 A resolution.In CopB-B crystals, a bound sulfate anion is identified at the phosphate-binding location. In solution state bound phosphate can be readily displaced by orthovanadate at submillimolar concentration as well as by sulfate at millimolar concentration. It is possible to assign the structure of the sulfate-bound phosphorylation domain of CopB-B to a state related to an enzyme/phosphate intermediate state of the catalytic cycle |
720230 |
| 7.2.2.9 | electron cryomicroscopy of two-dimensional crystals, projection map at 7 A resolution with density peaks |
688411 |
| 7.2.2.9 | hangimg drop vapour diffusion method, 3D crystals of CopB-B, the 29 kDa catalytic ATP binding/phosphorylation domain are produced, which diffracted to a resolution of 2.2 A |
719771 |
| 7.2.2.9 | solution structures of ATP-free and ATP-bound N-MNK |
712460 |
