4AGP

Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5176

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	CCD
Detector	ADSC CCD
Spacegroup name	P 21 21 21
Unit cell lengths	65.080, 71.170, 104.980
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.624 - 1.500
R-factor	0.1692
Rwork	0.168
R-free	0.18710
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	2j1x
RMSD bond length	0.006
RMSD bond angle	1.063
Phasing software	PHENIX
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.400	1.580
High resolution limit [Å]	1.500	1.500
Rmerge	0.070	0.230
Number of reflections	79145
<I/σ(I)>	16.3	6.7
Completeness [%]	99.9	99.9
Redundancy	5.7	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		294	SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM 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 KCL.