7B4B

Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273C mutant bound to MQ: R273C-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	68.730, 70.686, 85.107
Unit cell angles	90.00, 90.29, 90.00

Refinement procedure

Resolution	36.460 - 1.760
R-factor	0.1805
Rwork	0.179
R-free	0.21840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ibq
RMSD bond length	0.007
RMSD bond angle	0.845
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]	40.000	40.000	1.790
High resolution limit [Å]	1.760	4.770	1.760
Rmerge	0.113	0.083	0.574
Rmeas	0.129	0.095	0.658
Rpim	0.061	0.045	0.315
Total number of observations	327275
Number of reflections	78718	4067	3842
<I/σ(I)>	5.1
Completeness [%]	96.8	97	95.5
Redundancy	4.2	4.2	3.9
CC(1/2)		0.991	0.833

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	6.1	292	PROTEIN/DNA RATIO 1:2.4, 0.2M Sodium Fluoride, 20% w/v PEG 3350