6GGF

Structure of the p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9328

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-08-08
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.98
Spacegroup name	P 21 21 21
Unit cell lengths	65.110, 71.209, 105.351
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.608 - 1.320
R-factor	0.149570400365
Rwork	0.148
R-free	0.17082
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	2j1x
RMSD bond length	0.005
RMSD bond angle	0.818
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHENIX
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.610	1.390
High resolution limit [Å]	1.320	1.320
Rmerge	0.049	0.550
Number of reflections	114821
<I/σ(I)>	16	3.3
Completeness [%]	99.5	99.3
Redundancy	5.1	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm NaCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm NaCl.