7B4A
Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to DNA: R273H-DNA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-10-07 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.87290 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 136.784, 50.347, 67.481 |
| Unit cell angles | 90.00, 92.75, 90.00 |
Refinement procedure
| Resolution | 31.070 - 1.900 |
| R-factor | 0.2094 |
| Rwork | 0.207 |
| R-free | 0.25440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ibs |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.813 |
| 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] | 45.000 | 45.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 5.150 | 1.900 |
| Rmerge | 0.136 | 0.053 | 0.682 |
| Rmeas | 0.145 | 0.057 | 0.731 |
| Rpim | 0.051 | 0.020 | 0.259 |
| Total number of observations | 283631 | ||
| Number of reflections | 35603 | 1891 | 1781 |
| <I/σ(I)> | 4.5 | ||
| Completeness [%] | 98.2 | 99.5 | 98.5 |
| Redundancy | 8 | 7.9 | 7.9 |
| CC(1/2) | 0.998 | 0.934 |
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 |
