3QLG
Crystal structure of the L317I mutant of the C-src tyrosine kinase domain complexed with dasatinib
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-03-04 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 42.261, 63.494, 74.445 |
| Unit cell angles | 100.74, 90.18, 90.00 |
Refinement procedure
| Resolution | 34.476 - 2.750 |
| R-factor | 0.2033 |
| Rwork | 0.200 |
| R-free | 0.26850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3oez |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.944 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.2_432)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.476 | 2.900 |
| High resolution limit [Å] | 2.750 | 2.750 |
| Rmerge | 0.134 | 0.482 |
| Number of reflections | 18788 | |
| <I/σ(I)> | 12.05 | 3.1 |
| Completeness [%] | 95.1 | 87.3 |
| Redundancy | 3.9 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 287 | 7mg/ml protein, 0.25mM dasatinib, 0.1M MES, 0.2M sodium acetate, 4% Glycerol, 12% PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 287K |
