3H61
Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with norcantharidin (which is present in the structure in the hydrolyzed form)
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 | 2009-01-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97550 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 154.499, 41.781, 105.905 |
| Unit cell angles | 90.00, 96.96, 90.00 |
Refinement procedure
| Resolution | 37.500 - 1.450 |
| R-factor | 0.1643 |
| Rwork | 0.161 |
| R-free | 0.19375 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1s95 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.378 |
| 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] | 40.000 | 1.530 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.063 | 0.393 |
| Number of reflections | 115060 | |
| <I/σ(I)> | 200.1 | 3.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 2.6 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 10mM Tris-HC, 40% MPD, 20% PEG MME 5000 , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
