4R3P
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 | 143.828, 143.828, 143.828 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.482 - 2.905 |
R-factor | 0.211 |
Rwork | 0.208 |
R-free | 0.23980 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.884 |
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] | 45.482 | 45.488 | 3.037 |
High resolution limit [Å] | 2.900 | 4.609 | 2.905 |
Number of reflections | 11009 | ||
Completeness [%] | 99.2 | 97 | 100 |
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 |