7B4N
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 (II)
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 | 137.771, 49.982, 34.025 |
| Unit cell angles | 90.00, 93.23, 90.00 |
Refinement procedure
| Resolution | 46.980 - 1.320 |
| R-factor | 0.1422 |
| Rwork | 0.140 |
| R-free | 0.16550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ac0 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.057 |
| 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] | 100.000 | 100.000 | 1.340 |
| High resolution limit [Å] | 1.320 | 4.100 | 1.320 |
| Rmerge | 0.060 | 0.045 | 0.524 |
| Rmeas | 0.063 | 0.047 | 0.564 |
| Rpim | 0.018 | 0.014 | 0.203 |
| Total number of observations | 575464 | ||
| Number of reflections | 53678 | 1864 | 1730 |
| <I/σ(I)> | 8.8 | ||
| Completeness [%] | 99.3 | 99.1 | 97.5 |
| Redundancy | 10.7 | 11.4 | 6.8 |
| CC(1/2) | 0.999 | 0.895 |
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 |
