7B4B
Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273C mutant bound to MQ: R273C-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 | 68.730, 70.686, 85.107 |
| Unit cell angles | 90.00, 90.29, 90.00 |
Refinement procedure
| Resolution | 36.460 - 1.760 |
| R-factor | 0.1805 |
| Rwork | 0.179 |
| R-free | 0.21840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ibq |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.845 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2-3874) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 1.790 |
| High resolution limit [Å] | 1.760 | 4.770 | 1.760 |
| Rmerge | 0.113 | 0.083 | 0.574 |
| Rmeas | 0.129 | 0.095 | 0.658 |
| Rpim | 0.061 | 0.045 | 0.315 |
| Total number of observations | 327275 | ||
| Number of reflections | 78718 | 4067 | 3842 |
| <I/σ(I)> | 5.1 | ||
| Completeness [%] | 96.8 | 97 | 95.5 |
| Redundancy | 4.2 | 4.2 | 3.9 |
| CC(1/2) | 0.991 | 0.833 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6.1 | 292 | PROTEIN/DNA RATIO 1:2.4, 0.2M Sodium Fluoride, 20% w/v PEG 3350 |
