6HGT

Crystal structure of human KDM4A complexed with co-substrate analog NOG and histone H3 peptide with K9R mutation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04-1
Synchrotron site	Diamond
Beamline	I04-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-03-06
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9282
Spacegroup name	P 1 21 1
Unit cell lengths	58.440, 103.410, 144.520
Unit cell angles	90.00, 99.63, 90.00

Refinement procedure

Resolution	43.160 - 2.330
R-factor	0.252
Rwork	0.251
R-free	0.28000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2oq6
RMSD bond length	0.010
RMSD bond angle	1.050
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	BUSTER (2.10.3)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.270	2.390
High resolution limit [Å]	2.330	2.330
Rmerge	0.180	1.153
Number of reflections	72206	5294
<I/σ(I)>	8.6	1.6
Completeness [%]	99.7	100
Redundancy	6.5	7
CC(1/2)	0.984	0.560

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	Crystallisation solution is 0.1M Bis-Tris-Propane pH7.5, 12-16% PEG-4000. Co-substrate analog NOG and H3R9 peptide were co-crystallised with the protein.