7K1I
EGFR kinase (L858R/V948R) in complex with allosteric inhibitor JBJ-09-063
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-12-05 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 148.030, 35.800, 54.800 |
| Unit cell angles | 90.00, 100.19, 90.00 |
Refinement procedure
| Resolution | 53.936 - 3.202 |
| R-factor | 0.2656 |
| Rwork | 0.263 |
| R-free | 0.31060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5d41 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.818 |
| Data reduction software | xia2 |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 53.940 | 53.940 | 3.290 |
| High resolution limit [Å] | 3.200 | 14.320 | 3.200 |
| Rmerge | 0.144 | 0.077 | 0.922 |
| Rmeas | 0.158 | 0.085 | 1.010 |
| Rpim | 0.062 | 0.034 | 0.403 |
| Total number of observations | 31390 | 381 | 2049 |
| Number of reflections | 4805 | 66 | 351 |
| <I/σ(I)> | 7.2 | 14.9 | 1.3 |
| Completeness [%] | 98.8 | 98.1 | 96.3 |
| Redundancy | 6.5 | 5.8 | 5.8 |
| CC(1/2) | 0.994 | 0.992 | 0.721 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 0.1 M Bis-Tris pH 5.5, 28% (w/v) PEG 3350 |
