3DLM

Crystal structure of Tudor domain of human Histone-lysine N-methyltransferase SETDB1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ DW
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2008-06-20
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	54.518, 63.689, 69.083
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.830 - 1.770
R-factor	0.21
Rwork	0.208
R-free	0.23700
Structure solution method	SAD
RMSD bond length	0.013
RMSD bond angle	1.369
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXD
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.830
High resolution limit [Å]	1.770	3.810	1.770
Rmerge	0.049	0.039	0.178
Number of reflections	24050
<I/σ(I)>	42.6
Completeness [%]	99.7	99.1	99.6
Redundancy	6.9	6.8	6.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	1.5 microliter of the protein solution was mixed with 1.5 microliter of the reservoir solution containing 0.2 M Disodium tartrate, 20% PEG 3350 and 0.1M Hepes pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K