2EB2
Crystal structure of mutated EGFR kinase domain (G719S)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-08-06 |
Detector | MARRESEARCH |
Wavelength(s) | 0.97243 |
Spacegroup name | I 2 3 |
Unit cell lengths | 145.470, 145.470, 145.470 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.000 - 2.500 |
R-factor | 0.198 |
Rwork | 0.198 |
R-free | 0.25300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1m14 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 17866 | |
<I/σ(I)> | 35.357 | 9.75 |
Completeness [%] | 100.0 | 100 |
Redundancy | 43.094 | 33.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.1M MES, 1.1M Na/K tartrate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |