3QRJ
The crystal structure of human abl1 kinase domain T315I mutant in complex with DCC-2036
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] | 100 |
Detector technology | CCD |
Collection date | 2006-10-03 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.261, 59.435, 76.285 |
Unit cell angles | 90.00, 109.55, 90.00 |
Refinement procedure
Resolution | 19.590 - 1.820 |
R-factor | 0.232 |
Rwork | 0.229 |
R-free | 0.28600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Abl kinase |
RMSD bond length | 0.016 |
RMSD bond angle | 1.724 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.890 |
High resolution limit [Å] | 1.820 | 1.820 |
Rmerge | 0.408 | |
Number of reflections | 41838 | |
<I/σ(I)> | 16.1 | 2.2 |
Completeness [%] | 96.5 | 80.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.1 | 290 | 29% PEG 3350, 100MM BISTRIS PH 7.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K |