9S9O

Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt

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	2024-10-05
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.95374
Spacegroup name	P 21 21 21
Unit cell lengths	64.932, 71.138, 104.756
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.500 - 1.490
R-factor	0.152169221913
Rwork	0.150
R-free	0.18560
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.005
RMSD bond angle	0.772
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]	29.500	1.510
High resolution limit [Å]	1.490	1.490
Rmerge	0.057	0.742
Rpim	0.017	0.224
Number of reflections	78956	3791
<I/σ(I)>	23.9	3.6
Completeness [%]	98.7
Redundancy	11.4
CC(1/2)	1.000	0.877

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: 18 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