5HCX
EGFR kinase domain mutant "TMLR" with azabenzimidazole compound 7
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] | 110 |
Detector technology | CCD |
Collection date | 2013-12-11 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9774 |
Spacegroup name | I 2 3 |
Unit cell lengths | 146.744, 146.744, 146.744 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.080 - 2.600 |
R-factor | 0.1935 |
Rwork | 0.192 |
R-free | 0.22290 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB 5EM5 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.090 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | BUSTER (2.11.4) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.080 | 2.700 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.816 | |
Number of reflections | 15892 | |
<I/σ(I)> | 16.7 | 2.2 |
Completeness [%] | 98.0 | 99.5 |
Redundancy | 6.2 | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 292 | PEG 10K, ethylene glycol |