4R3R
Crystal structures of EGFR in complex with Mig6
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 | CCD |
Collection date | 2012-11-14 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97920 |
Spacegroup name | I 2 3 |
Unit cell lengths | 144.689, 144.689, 144.689 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.755 - 3.250 |
R-factor | 0.2009 |
Rwork | 0.196 |
R-free | 0.24680 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.947 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASES |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 45.750 | 3.500 |
High resolution limit [Å] | 3.260 | 5.550 | 3.250 |
Number of reflections | 7110 | ||
Completeness [%] | 87.8 | 82 | 92 |
Redundancy | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 40% PEG400, 0.15M SODIUM CHLORIDE, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |