5SWH
c-Src V281C kinase domain in complex with Rao-IV-151
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-06-02 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97946 |
| Spacegroup name | P 1 |
| Unit cell lengths | 41.819, 64.139, 74.910 |
| Unit cell angles | 77.94, 89.50, 89.83 |
Refinement procedure
| Resolution | 73.250 - 2.500 |
| R-factor | 0.2435 |
| Rwork | 0.241 |
| R-free | 0.28710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3uqg |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.528 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.25) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 73.250 | 73.250 | 2.600 |
| High resolution limit [Å] | 2.500 | 9.010 | 2.500 |
| Rmerge | 0.186 | 0.054 | 1.225 |
| Rmeas | 0.201 | ||
| Rpim | 0.075 | ||
| Total number of observations | 149393 | ||
| Number of reflections | 21164 | ||
| <I/σ(I)> | 8.5 | ||
| Completeness [%] | 80.3 | 82.7 | 80.8 |
| Redundancy | 7.1 | 7.1 | 7 |
| CC(1/2) | 0.994 | 0.997 | 0.577 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | 100 mM MES pH 6, 8% PEG 3350, 3% glycerol, 10 mM DTT, 10 mM NaOAc |
