3H62
Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with cantharidic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-03-12 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.93340 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 154.535, 41.518, 97.502 |
| Unit cell angles | 90.00, 103.44, 90.00 |
Refinement procedure
| Resolution | 36.080 - 1.400 |
| R-factor | 0.17901 |
| Rwork | 0.176 |
| R-free | 0.20392 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1s95 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.308 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0089) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.470 | 1.480 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.078 | 0.347 |
| Number of reflections | 113739 | |
| <I/σ(I)> | 60.1 | 13.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.6 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
