7B47

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

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	2017-03-02
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97200
Spacegroup name	P 1 21 1
Unit cell lengths	69.043, 71.000, 85.115
Unit cell angles	90.00, 90.34, 90.00

Refinement procedure

Resolution	49.500 - 1.800
R-factor	0.1782
Rwork	0.178
R-free	0.20180
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ibs
RMSD bond length	0.005
RMSD bond angle	0.901
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX (1.18.2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.830
High resolution limit [Å]	1.800	4.880	1.800
Rmerge	0.066	0.048	0.493
Rmeas	0.075	0.055	0.559
Rpim	0.034	0.026	0.258
Total number of observations	333432
Number of reflections	76162	3907	3811
<I/σ(I)>	9
Completeness [%]	99.4	98.7	99.5
Redundancy	4.4	4.4	4.2
CC(1/2)		0.996	0.905

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	6.1	292	0.1M Li Acetate, 16% w/v PEG 3350