8Q1S
Pathogenic mutations of human phosphorylation sites affect protein-protein interactions
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-12-06 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 123.780, 123.780, 250.200 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.700 - 3.230 |
| R-factor | 0.23286 |
| Rwork | 0.230 |
| R-free | 0.27937 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 1.132 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.700 | 3.420 |
| High resolution limit [Å] | 3.230 | 3.230 |
| Rmeas | 0.035 | 0.296 |
| Number of reflections | 22972 | 3708 |
| <I/σ(I)> | 6.91 | |
| Completeness [%] | 99.9 | |
| Redundancy | 10.39 | |
| CC(1/2) | 0.995 | 0.368 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 19% PEG 3350, 0.35 M NaBr, 0.1 M BisTris-Propane pH 6.5 |
