3H60
Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Mn2+ atoms
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.89225 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 154.414, 41.755, 105.432 |
| Unit cell angles | 90.00, 97.07, 90.00 |
Refinement procedure
| Resolution | 65.800 - 2.000 |
| R-factor | 0.16653 |
| Rwork | 0.161 |
| R-free | 0.21859 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1s95 |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.830 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.4.0067) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.800 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.099 | 0.285 |
| Number of reflections | 44744 | |
| <I/σ(I)> | 14.8 | 5.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.6 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 10mM Tris-HCl, MPD 40%, PEG MME 5000 20%, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
