7B48

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-07-22
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.87290
Spacegroup name	P 1 21 1
Unit cell lengths	69.249, 72.003, 85.233
Unit cell angles	90.00, 90.07, 90.00

Refinement procedure

Resolution	36.670 - 2.050
R-factor	0.1787
Rwork	0.176
R-free	0.22750
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ibs
RMSD bond length	0.014
RMSD bond angle	2.012
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0266)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	39.000	39.000	2.090
High resolution limit [Å]	2.050	5.560	2.050
Rmerge	0.114	0.083	0.254
Rmeas	0.136	0.100	0.303
Rpim	0.073	0.054	0.162
Number of reflections	49698	2603	2127
<I/σ(I)>	10.18
Completeness [%]	94.2	95.1	81.1
Redundancy	3.1	3.1	3
CC(1/2)	0.986	0.988	0.910

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	6.1	292	0.2M Li Acetate, 2.0% w/v Agarose, 20% w/v PEG 3350