2X0V

STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO 4-(trifluoromethyl)benzene-1,2-diamine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Detector	ADSC CCD
Spacegroup name	P 21 21 21
Unit cell lengths	65.226, 71.088, 105.389
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.030 - 1.800
R-factor	0.1635
Rwork	0.162
R-free	0.18900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2j1x
RMSD bond length	0.005
RMSD bond angle	0.904
Phasing software	PHENIX
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.100	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.060	0.220
Number of reflections	45419
<I/σ(I)>	14.2	5.5
Completeness [%]	98.7	97.9
Redundancy	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.2	294	SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. 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 % PEG 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF SMALL MOLECULE LIGAND IN 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19 % PEG 4000, 20 % GLYCEROL, 150 MM KCL.