2IE4
Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-07-15 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.9796 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 92.540, 194.850, 201.350 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.600 |
| R-factor | 0.26 |
| Rwork | 0.270 |
| R-free | 0.23000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.600 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.700 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.465 | |
| Number of reflections | 62598 | |
| Completeness [%] | 99.4 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.2 mM lithium sulfate, 1.5 M ammonium sulfate, 0.1 M Tris-Cl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
