9S9Q

Crystal structure of p53 cancer mutant Y220N 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 X 16M
Wavelength(s)	0.97628
Spacegroup name	P 21 21 21
Unit cell lengths	65.075, 71.150, 104.597
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.000 - 1.870
R-factor	0.198481625995
Rwork	0.196
R-free	0.24251
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.006
RMSD bond angle	0.831
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]	52.300	1.910
High resolution limit [Å]	1.870	1.870
Rmerge	0.162	1.021
Rpim	0.056	0.349
Number of reflections	40660	2555
<I/σ(I)>	8	2.1
Completeness [%]	99.5	99.7
Redundancy	9.1	9.4
CC(1/2)	0.998	0.882

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: 10% PEG 8000, 8% ethylene glycol, 0.1 M HEPES pH 7.5 (protein:buffer 1:1). Cryo: reservoir buffer supplemented with 23% ethylene glycol.