4QUM
Crystal structure of PTPN3 (PTPH1) in complex with a dually phosphorylated MAPK12 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL15A1 |
| Synchrotron site | NSRRC |
| Beamline | BL15A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-03-06 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 75.491, 75.491, 109.605 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 31.325 - 2.516 |
| R-factor | 0.1993 |
| Rwork | 0.197 |
| R-free | 0.24480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2b49 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.252 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASES |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.600 |
| High resolution limit [Å] | 2.510 | 2.510 |
| Rmerge | 0.122 | 0.521 |
| Number of reflections | 12505 | |
| <I/σ(I)> | 10.79 | 2.35 |
| Completeness [%] | 98.0 | 95.1 |
| Redundancy | 4.7 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1M Tris-HCl, 30% PEG 8000, 5% glycerol, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
