7LG8
EGFR (T79M/V948R) in complex with naquotinib and an allosteric inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-12-05 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.654, 75.947, 150.978 |
| Unit cell angles | 90.00, 94.41, 90.00 |
Refinement procedure
| Resolution | 50.810 - 2.930 |
| R-factor | 0.2371 |
| Rwork | 0.235 |
| R-free | 0.26960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6duk |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.777 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.19_4080) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.810 | 50.820 | 2.980 |
| High resolution limit [Å] | 2.930 | 7.930 | 2.930 |
| Rmeas | 0.265 | 0.073 | 1.442 |
| Rpim | 0.133 | 0.037 | 0.745 |
| Total number of observations | 102045 | 5088 | 3860 |
| Number of reflections | 26936 | 1405 | 1146 |
| <I/σ(I)> | 4.2 | 16.5 | 0.6 |
| Completeness [%] | 98.5 | 99 | 85.8 |
| Redundancy | 3.8 | 3.6 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 0.1 M Bis-Tris pH 5.5, 30% (w/v) PEG 3350 |
