2ITT
Crystal structure of EGFR kinase domain L858R mutation in complex with AEE788
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-08-05 |
| Detector | ADSC QUANTUM-4 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 145.717, 145.717, 145.717 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.990 - 2.730 |
| R-factor | 0.212 |
| Rwork | 0.208 |
| R-free | 0.26200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m17 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.809 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.940 |
| High resolution limit [Å] | 2.730 | 2.730 |
| Rmerge | 0.050 | 0.370 |
| Number of reflections | 13877 | |
| <I/σ(I)> | 36.2 | 4.3 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 6.1 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 40% PEG400, 0.15M NACL, 0.1M HEPES 8.0, pH 7.5 |
