3UE4
Structural and spectroscopic analysis of the kinase inhibitor bosutinib binding to the Abl tyrosine kinase domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 77 |
Detector technology | PIXEL |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.9795 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 56.860, 113.760, 127.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 63.820 - 2.424 |
R-factor | 0.192 |
Rwork | 0.188 |
R-free | 0.24870 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.059 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | PHENIX ((phenix.refine: 1.7_650)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 63.820 | 2.560 |
High resolution limit [Å] | 2.424 | 2.424 |
Rmerge | 0.112 | 0.552 |
Number of reflections | 18506 | |
<I/σ(I)> | 13.5 | 3.1 |
Completeness [%] | 93.8 | 94.8 |
Redundancy | 5.9 | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 0.1M Ammonium Acetate 0.1M BisTris pH 5.5 11% PEG 10K, VAPOR DIFFUSION, HANGING DROP, temperature 298K |