9S9P

Crystal structure of p53 cancer mutant Y220S 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 I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-11-15
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.97628
Spacegroup name	P 21 21 21
Unit cell lengths	64.780, 70.991, 104.645
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.900 - 1.400
R-factor	0.163011235977
Rwork	0.162
R-free	0.18840
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.005
RMSD bond angle	0.789
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]	55.100	1.420
High resolution limit [Å]	1.400	1.400
Rmerge	0.066	0.710
Number of reflections	95141	4376
<I/σ(I)>	16.2	2
Completeness [%]	99.5	94
Redundancy	9.4	6.3
CC(1/2)	0.999	0.759

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein solution: 6 mg/ml in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP, 1 mM Rezatapopt, 2% DMSO. Reservoir buffer: 0.2 M ammonium nitrate, 20% PEG 3350 (protein:buffer 2:1). Cryo: reservoir buffer supplemented with 23% ethylene glycol.