5G4O

Crystal structure of the p53 cancer mutant Y220C in complex with a trifluorinated derivative of the small molecule stabilizer Phikan083

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Spacegroup name	P 21 21 21
Unit cell lengths	65.162, 71.448, 105.235
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.534 - 1.480
R-factor	0.145
Rwork	0.144
R-free	0.17140
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2j1x
RMSD bond length	0.005
RMSD bond angle	0.802
Phasing software	PHENIX
Refinement software	PHENIX ((DEV_2386: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.600	1.560
High resolution limit [Å]	1.480	1.480
Rmerge	0.050	0.490
Number of reflections	82444
<I/σ(I)>	16.5	3.7
Completeness [%]	99.9	100
Redundancy	5.4	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: 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 KCL.