2ITY
Crystal structure of EGFR kinase domain in complex with Iressa
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-12-03 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | I 2 3 |
Unit cell lengths | 145.140, 145.140, 145.140 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.890 - 3.420 |
R-factor | 0.216 |
Rwork | 0.211 |
R-free | 0.26000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1m17 |
RMSD bond length | 0.022 |
RMSD bond angle | 1.811 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.680 |
High resolution limit [Å] | 3.420 | 3.420 |
Rmerge | 0.120 | 0.400 |
Number of reflections | 6996 | |
<I/σ(I)> | 19.1 | 5.8 |
Completeness [%] | 99.7 | 100 |
Redundancy | 7.2 | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 1.2M KNA TARTRATE, 0.1M HEPES 7.5, pH 7.50 |