7B49
Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to DNA and MQ: R273H-DNA-MQ
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 | 2018-12-08 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97200 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 136.685, 50.056, 68.353 |
| Unit cell angles | 90.00, 93.56, 90.00 |
Refinement procedure
| Resolution | 34.110 - 1.420 |
| R-factor | 0.1865 |
| Rwork | 0.184 |
| R-free | 0.22940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ibs |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.043 |
| 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] | 39.000 | 39.000 | 1.400 |
| High resolution limit [Å] | 1.380 | 3.740 | 1.380 |
| Rmerge | 0.119 | 0.058 | 0.618 |
| Rmeas | 0.132 | 0.064 | 0.686 |
| Rpim | 0.055 | 0.027 | 0.293 |
| Total number of observations | 510562 | ||
| Number of reflections | 93002 | 4805 | 4616 |
| <I/σ(I)> | 3.6 | ||
| Completeness [%] | 98.0 | 97.7 | 97.8 |
| Redundancy | 5.5 | 5.8 | 5.1 |
| CC(1/2) | 0.997 | 0.587 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6.1 | 292 | Protein/DNA ratio 1:1.4, 0.075M Sodium formate, 7.5% w/v PEG 3350 |
