4I23
Crystal structure of the wild-type EGFR kinase domain in complex with dacomitinib (soaked)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 98 |
Detector technology | CCD |
Collection date | 2011-01-21 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | I 2 3 |
Unit cell lengths | 146.342, 146.342, 146.342 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.920 - 2.800 |
R-factor | 0.229 |
Rwork | 0.226 |
R-free | 0.27900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 0.900 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNX |
Refinement software | CNX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.076 | 0.579 |
Number of reflections | 13020 | |
<I/σ(I)> | 26.5 | 5.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 9.91 | 10.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 294 | 1.2-1.4 M Na-K Tartrate 0.1 M MES, pH 6.9-7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K |