4G9J
Protein Ser/Thr phosphatase-1 in complex with cell-permeable peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-12-15 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.1271 |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 138.007, 138.007, 113.675 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 97.586 - 3.100 |
| R-factor | 0.226 |
| Rwork | 0.224 |
| R-free | 0.27600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fjm |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.022 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.2.19) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 97.586 | 49.110 | 3.330 |
| High resolution limit [Å] | 3.000 | 9.990 | 3.160 |
| Rmerge | 0.127 | 0.040 | 0.664 |
| Total number of observations | 3504 | 16250 | |
| Number of reflections | 22186 | ||
| <I/σ(I)> | 11.2 | 13.2 | 1.2 |
| Completeness [%] | 99.0 | 96.3 | 99.7 |
| Redundancy | 5.9 | 5.2 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | SITTING DROP | 8 | 293 | 20% PEG6000, 1 M lithium chloride, pH 8.0, SITTING DROP, temperature 293K |
