2X0W

STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO 5,6-dimethoxy- 2-methylbenzothiazole

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Detector	ADSC CCD
Spacegroup name	P 21 21 21
Unit cell lengths	65.250, 70.580, 105.440
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.903 - 2.100
R-factor	0.175
Rwork	0.172
R-free	0.22800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2j1x
RMSD bond length	0.007
RMSD bond angle	0.986
Phasing software	PHENIX
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.500	2.210
High resolution limit [Å]	2.100	2.100
Rmerge	0.110	0.290
Number of reflections	29108
<I/σ(I)>	8.6	4.1
Completeness [%]	99.9	100
Redundancy	3.5	3.6

Crystallization Conditions

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