7B4F
Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R282W mutant bound to DNA: R282W-MQ (I)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-03-10 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54178 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 137.210, 49.743, 33.816 |
Unit cell angles | 90.00, 93.36, 90.00 |
Refinement procedure
Resolution | 18.420 - 1.780 |
R-factor | 0.1592 |
Rwork | 0.155 |
R-free | 0.19540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ac0 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.723 |
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] | 21.000 | 21.000 | 1.810 |
High resolution limit [Å] | 1.780 | 4.810 | 1.780 |
Rmerge | 0.067 | 0.031 | 0.452 |
Rmeas | 0.076 | 0.035 | 0.509 |
Rpim | 0.034 | 0.016 | 0.233 |
Total number of observations | 100983 | ||
Number of reflections | 21071 | 1130 | 961 |
<I/σ(I)> | 11.8 | ||
Completeness [%] | 95.9 | 98.8 | 92.3 |
Redundancy | 4.8 | 4.6 | 4.6 |
CC(1/2) | 0.999 | 0.877 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 292 | Protein/DNA ratio 1:1.5, 0.03M Citric acid, 0.07M BIS-TRIS propane pH=7.6, 20% w/v PEG 3350 |