5KYK
Covalent GTP-competitive inhibitors of KRAS G12C: Guanosine bisphosphonate Analogs
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 114.830, 66.155, 98.006 |
| Unit cell angles | 90.00, 112.98, 90.00 |
Refinement procedure
| Resolution | 43.741 - 2.702 |
| R-factor | 0.2695 |
| Rwork | 0.267 |
| R-free | 0.31440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nmm |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.478 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.700 |
| High resolution limit [Å] | 2.650 | 7.190 | 2.650 |
| Rmerge | 0.073 | 0.039 | |
| Rmeas | 0.078 | 0.043 | |
| Rpim | 0.033 | 0.017 | 0.696 |
| Total number of observations | 126113 | ||
| Number of reflections | 19876 | ||
| <I/σ(I)> | 9.3 | ||
| Completeness [%] | 99.8 | 99 | 98.1 |
| Redundancy | 6.3 | 6.2 | 4.6 |
| CC(1/2) | 0.998 | 0.459 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 293 | Protein was purified in buffer: 20 mM Hepes pH 8.0, 150 mM NaCl, 5 mM MgCl2 and 0.5 mM DTT. Crystals grew in five days at room temperature from hanging vapor diffusion drops with following condition: 0.1 M Citric acid pH 4.0, 20% PEG 3350. Crystals were cryoprotected in mother liquid with 40% PEG 3350 and flash frozen in liquid nitrogen. |
