9S9N

Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt analog 8

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-08-04
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.97627
Spacegroup name	P 21 21 21
Unit cell lengths	64.801, 71.054, 104.669
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	55.100 - 1.720
R-factor	0.1613206431
Rwork	0.159
R-free	0.20688
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.006
RMSD bond angle	0.777
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	104.700	1.750
High resolution limit [Å]	1.720	1.720
Rmerge	0.085	1.355
Number of reflections	52064	2726
<I/σ(I)>	17.7	1.9
Completeness [%]	99.9	99.7
Redundancy	13.6	13.1
CC(1/2)	1.000	0.913

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein solution: 6 mg/ml protein in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mM Hepes, pH 7.0, 19% (w/v) polyethylene glycol 4000. Soaking buffer: 17 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.