7B47
Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to MQ: R273H-MQ (I)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-03-02 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97200 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.043, 71.000, 85.115 |
| Unit cell angles | 90.00, 90.34, 90.00 |
Refinement procedure
| Resolution | 49.500 - 1.800 |
| R-factor | 0.1782 |
| Rwork | 0.178 |
| R-free | 0.20180 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ibs |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.901 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.066 | 0.048 | 0.493 |
| Rmeas | 0.075 | 0.055 | 0.559 |
| Rpim | 0.034 | 0.026 | 0.258 |
| Total number of observations | 333432 | ||
| Number of reflections | 76162 | 3907 | 3811 |
| <I/σ(I)> | 9 | ||
| Completeness [%] | 99.4 | 98.7 | 99.5 |
| Redundancy | 4.4 | 4.4 | 4.2 |
| CC(1/2) | 0.996 | 0.905 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6.1 | 292 | 0.1M Li Acetate, 16% w/v PEG 3350 |
