9S9L

Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt precursor

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-02-06
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.999977
Spacegroup name	P 21 21 21
Unit cell lengths	64.766, 71.245, 104.588
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.900 - 1.380
R-factor	0.149671068117
Rwork	0.148
R-free	0.17415
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]	47.900	1.400
High resolution limit [Å]	1.300	1.380
Rmerge	0.051	0.945
Number of reflections	99954	4875
<I/σ(I)>	17.7	2.1
Completeness [%]	99.9	100
Redundancy	6.6	6.8
CC(1/2)	1.000	0.783

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	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: 19 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.