7B4H
Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human wild-type p53DBD bound to DNA and MQ: wt-DNA-MQ (III)
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 | 2014-04-27 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97600 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 137.564, 50.104, 34.100 |
| Unit cell angles | 90.00, 92.97, 90.00 |
Refinement procedure
| Resolution | 47.070 - 1.390 |
| R-factor | 0.1708 |
| Rwork | 0.169 |
| R-free | 0.20040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ac0 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.875 |
| 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] | 49.000 | 49.000 | 1.410 |
| High resolution limit [Å] | 1.390 | 3.770 | 1.390 |
| Rmerge | 0.093 | 0.067 | 0.559 |
| Rmeas | 0.100 | 0.072 | 0.604 |
| Rpim | 0.036 | 0.027 | 0.225 |
| Total number of observations | 339531 | ||
| Number of reflections | 46808 | 2418 | 2318 |
| <I/σ(I)> | 6.1 | ||
| Completeness [%] | 99.7 | 99.8 | 99.2 |
| Redundancy | 7.3 | 7.3 | 6.7 |
| CC(1/2) | 0.995 | 0.857 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 292 | Protein/DNA ratio 1:2.4, 0.1M TRIS pH=8.5, 2% Tacsimate(TM) pH=8.0, 16% w/v PEG 3350 |
