8CG7

Structure of p53 cancer mutant Y220C with arylation at Cys182 and Cys277

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	2020-12-18
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	64.881, 71.046, 104.887
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.900 - 1.530
R-factor	0.159423360227
Rwork	0.158
R-free	0.18720
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.785
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	1.560
High resolution limit [Å]	1.530	1.530
Rmerge	0.046	0.801
Rmeas	0.051	0.880
Number of reflections	73231	3553
<I/σ(I)>	17.6	2.3
Completeness [%]	99.4	99.4
Redundancy	5.6	5.7
CC(1/2)	1.000	0.892

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein solution: 6 mg/ml in 25 mM phosphate buffer, pH 7.2, 0.5 mM TCEP. Crystallization buffer: 19% polyethylene glycol 4000, 100 mM Hepes, pH 7.0. For covalent modification, crystals were soaked for 4 hours in crystallization buffer complemented with 20% glycerol and 30 mM compound before flash freezing in liquid nitrogen.