6V90

Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 12

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID30B
Synchrotron site	ESRF
Beamline	ID30B
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-04-12
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.96770
Spacegroup name	C 2 2 21
Unit cell lengths	45.360, 104.639, 168.863
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.470 - 2.040
R-factor	0.1996
Rwork	0.198
R-free	0.24100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	internal
RMSD bond length	0.014
RMSD bond angle	1.617
Data reduction software	XDS
Data scaling software	Aimless (0.6.3)
Phasing software	PHASER
Refinement software	REFMAC (5.8.0189)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.470	2.110
High resolution limit [Å]	2.040	2.040
Rmerge	0.059	1.359
Rmeas	0.064	1.465
Rpim	0.025	0.543
Total number of observations		17856
Number of reflections	26016	2497
<I/σ(I)>	17.4	1.5
Completeness [%]	99.6	99.8
Redundancy	6.8	7.2
CC(1/2)	0.999	0.603

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		277	INDEX F6. 0.1 M Bis-Tris pH 5.5, 0.2 M ammonium sulfate 25% w/v PEG 3350. The crystal was cryoprotected with MiTeGen Low Viscosity Cryo Oil