9FL8
Stapled peptide bound to NOT9-NOT1 complex
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 | PIXEL |
| Collection date | 2022-09-09 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.88560 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 106.562, 106.562, 262.572 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.140 - 2.640 |
| R-factor | 0.2052 |
| Rwork | 0.203 |
| R-free | 0.24950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.653 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 131.286 | 2.970 |
| High resolution limit [Å] | 2.640 | 2.645 |
| Rmerge | 0.202 | 1.968 |
| Rmeas | 0.208 | 2.020 |
| Rpim | 0.047 | 0.450 |
| Total number of observations | 25814 | |
| Number of reflections | 26138 | 1307 |
| <I/σ(I)> | 10.4 | 1.8 |
| Completeness [%] | 50.7 | |
| Redundancy | 19.1 | 19.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5 | 298 | 2M sodium formate, 0.1M sodium acetate |
