4RIY
Crystal structure of an EGFR/HER3 kinase domain heterodimer containing the cancer-associated HER3-E909G mutation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-07-27 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.115867 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.334, 155.140, 87.297 |
| Unit cell angles | 90.00, 110.93, 90.00 |
Refinement procedure
| Resolution | 56.200 - 2.981 |
| R-factor | 0.2212 |
| Rwork | 0.216 |
| R-free | 0.26700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2GS6 AND 3KEX |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.093 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.000 | 3.210 |
| High resolution limit [Å] | 2.981 | 3.000 |
| Rmerge | 0.176 | 0.573 |
| Number of reflections | 32340 | |
| <I/σ(I)> | 6.5 | 2.7 |
| Completeness [%] | 99.5 | 99.9 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 10 mg/mL protein, 0.1M HEPES pH 7.5, 15% PEG-5000 MME, 5mM magnesium chloride, 0.5M ammonium acetate, 2mM AMP-PNP, 1mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
