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