6V8K

Crystal structure of the p300 acetyltransferase domain with peptide-competitive inhibitor 2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-02-10
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	1.12723
Spacegroup name	P 43
Unit cell lengths	60.669, 60.669, 100.647
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	60.670 - 1.840
R-factor	0.1804
Rwork	0.179
R-free	0.21340
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	internal
RMSD bond length	0.011
RMSD bond angle	1.500
Data reduction software	XDS
Data scaling software	Aimless (0.5.31)
Phasing software	PHASER
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.650	1.940
High resolution limit [Å]	1.840	1.840
Rmerge	0.038	0.441
Rmeas	0.047	0.522
Rpim	0.018	0.204
Total number of observations	172283	12431
Number of reflections	26347	2150
<I/σ(I)>	21.9	1.8
Completeness [%]	83.2	46.9
Redundancy	6.5	5.8
CC(1/2)	0.997	0.931

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	277	0.24 mM HAT, 0.12 mM CoA, 0.75 mM ligand. 200+150 (+20) nL sitting drops. Internal focus screen with microseeding. 17.5% MPD, 0.1 M Tris pH 8, 2.5 % PEG3350. Cryo 30% MPD, 5% PEG 3350, 1 mM ligand