2YBG

Structure of Lys120-acetylated p53 core domain

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 1 21 1
Unit cell lengths	68.926, 69.581, 83.494
Unit cell angles	90.00, 90.12, 90.00

Refinement procedure

Resolution	42.212 - 1.900
R-factor	0.1768
Rwork	0.174
R-free	0.22600
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.970
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.000	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.080	0.340
Number of reflections	60047
<I/σ(I)>	7.5	2.4
Completeness [%]	96.6	98.8
Redundancy	2	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1				PROTEIN SOLUTION: 5 MG/ML PROTEIN IN 20 MM CITRATE BUFFER PH 6.1, 150 MM NACL, 10 MM DTT. CRYSTALLIZATION BUFFER: 26% (W/V) PEG 3350, 43 MM SODIUM ACETATE AND 100 MM HEPES, PH 7.5