4LI5
EGFR-K IN COMPLEX WITH N-[3-[[5-chloro-4-(1H-indol-3-yl)pyrimidin-2-yl]amino]-4-methoxy-phenyl] Prop-2-enamide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2010-07-05 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 144.892, 144.892, 144.892 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 102.600 - 2.640 |
| R-factor | 0.16599 |
| Rwork | 0.165 |
| R-free | 0.20299 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.045 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 102.600 | 2.780 |
| High resolution limit [Å] | 2.630 | 2.640 |
| Rmerge | 0.092 | 0.697 |
| Number of reflections | 15026 | |
| <I/σ(I)> | 32.02 | 9.75 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 24.4 | 25.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 4.6 | 293 | The protein at 6 mg/ml was crystallized from 0.2 M NH4Cl, 1.2 M Na-K-tartrate buffered with 10mM acetate at pH 4.6 and 0.15M Hepes pH 7.0, VAPOR DIFFUSION, temperature 293K |
