5IOH
RepoMan-PP1a (protein phosphatase 1, alpha isoform) holoenzyme complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-11-12 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 160.769, 57.089, 73.635 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.545 - 2.566 |
| R-factor | 0.1785 |
| Rwork | 0.176 |
| R-free | 0.21520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4mov |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.610 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.640 |
| High resolution limit [Å] | 2.566 | 2.600 |
| Rmerge | 0.017 | |
| Number of reflections | 22441 | |
| <I/σ(I)> | 15.3 | 2.4 |
| Completeness [%] | 99.3 | 90.4 |
| Redundancy | 11.5 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 277 | 100 mM Sodium Malonate, 12% PEG 3350 |
