7B4E

Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R282W mutant bound to DNA and MQ: R282W-DNA-MQ

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	2018-08-07
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.96770
Spacegroup name	C 1 2 1
Unit cell lengths	136.505, 49.553, 33.401
Unit cell angles	90.00, 93.44, 90.00

Refinement procedure

Resolution	34.060 - 1.580
R-factor	0.1684
Rwork	0.166
R-free	0.20130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ac0
RMSD bond length	0.006
RMSD bond angle	1.050
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]	50.000	50.000	1.610
High resolution limit [Å]	1.570	4.290	1.580
Rmerge	0.111	0.059	0.610
Rmeas	0.116	0.062	0.685
Rpim	0.034	0.018	0.304
Number of reflections	30188	1605	1443
<I/σ(I)>	6.3
Completeness [%]	97.5	99.8	93.5
Redundancy	10.1	11.9	4.4
CC(1/2)		0.998	0.716

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	6.1	292	Protein/DNA ratio 1:1.5, 0.1M Sodium Acetate, 20% w/v PEG 3350