5AOM

Structure of the p53 cancer mutant Y220C with bound small molecule PhiKan883

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Spacegroup name	P 21 21 21
Unit cell lengths	65.160, 71.270, 105.110
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.731 - 1.740
R-factor	0.1696
Rwork	0.169
R-free	0.19120
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2j1x
RMSD bond length	0.007
RMSD bond angle	1.026
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.700	1.830
High resolution limit [Å]	1.740	1.740
Rmerge	0.070	0.350
Number of reflections	49879
<I/σ(I)>	14.9	4.7
Completeness [%]	98.2	96.7
Redundancy	5.6	5.4

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.