7B49

Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to DNA and MQ: R273H-DNA-MQ

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	2018-12-08
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97200
Spacegroup name	C 1 2 1
Unit cell lengths	136.685, 50.056, 68.353
Unit cell angles	90.00, 93.56, 90.00

Refinement procedure

Resolution	34.110 - 1.420
R-factor	0.1865
Rwork	0.184
R-free	0.22940
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ibs
RMSD bond length	0.008
RMSD bond angle	1.043
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]	39.000	39.000	1.400
High resolution limit [Å]	1.380	3.740	1.380
Rmerge	0.119	0.058	0.618
Rmeas	0.132	0.064	0.686
Rpim	0.055	0.027	0.293
Total number of observations	510562
Number of reflections	93002	4805	4616
<I/σ(I)>	3.6
Completeness [%]	98.0	97.7	97.8
Redundancy	5.5	5.8	5.1
CC(1/2)		0.997	0.587

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