5X26
Crystal structure of EGFR 696-1022 L858R in complex with SKLB(3)
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 | 2011-04-06 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97923 |
Spacegroup name | I 2 3 |
Unit cell lengths | 145.278, 145.278, 145.278 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.827 - 2.951 |
R-factor | 0.1969 |
Rwork | 0.196 |
R-free | 0.22150 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2itv |
RMSD bond length | 0.014 |
RMSD bond angle | 1.277 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.950 |
Number of reflections | 10731 |
<I/σ(I)> | 14.6 |
Completeness [%] | 98.2 |
Redundancy | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.1M Hepes pH7.8, 40% PEG400, 0.15M NaCl, 5mM tris(2-carboxyethyl)-phosphine (TCEP) |