7B48
Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to MQ: R273H-MQ (II)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-07-22 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.87290 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.249, 72.003, 85.233 |
Unit cell angles | 90.00, 90.07, 90.00 |
Refinement procedure
Resolution | 36.670 - 2.050 |
R-factor | 0.1787 |
Rwork | 0.176 |
R-free | 0.22750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ibs |
RMSD bond length | 0.014 |
RMSD bond angle | 2.012 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0266) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 39.000 | 39.000 | 2.090 |
High resolution limit [Å] | 2.050 | 5.560 | 2.050 |
Rmerge | 0.114 | 0.083 | 0.254 |
Rmeas | 0.136 | 0.100 | 0.303 |
Rpim | 0.073 | 0.054 | 0.162 |
Number of reflections | 49698 | 2603 | 2127 |
<I/σ(I)> | 10.18 | ||
Completeness [%] | 94.2 | 95.1 | 81.1 |
Redundancy | 3.1 | 3.1 | 3 |
CC(1/2) | 0.986 | 0.988 | 0.910 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 6.1 | 292 | 0.2M Li Acetate, 2.0% w/v Agarose, 20% w/v PEG 3350 |