1H3I

Crystal structure of the Histone Methyltransferase SET7/9

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Detector	ADSC CCD
Wavelength(s)	0.9794, 0.9394, 0.9800
Spacegroup name	P 21 21 21
Unit cell lengths	66.090, 82.830, 116.150
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 * - 2.100
R-factor	0.212
Rwork	0.210
R-free	0.25800 *
Structure solution method	MAD
RMSD bond length	0.010
RMSD bond angle	1.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall
Low resolution limit [Å]	30.000 *
High resolution limit [Å]	2.100
Rmerge	0.048 *
Number of reflections	37053
Completeness [%]	84.0 *
Redundancy	3.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7		pH 7.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris	50 (mM)	pH7.0
3	1	drop		100 (mM)
4	1	drop	TCEP	1 (mM)
5	1	reservoir	magnesium formate	0.2 (M)
6	1	reservoir	PEG3350	25 (%)