1MLV

Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	95
Detector technology	IMAGE PLATE
Collection date	2002-08-02
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	I 2 2 2
Unit cell lengths	132.160, 156.680, 268.440
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.000 * - 2.600
Rwork	0.232
R-free	0.27800 *
Structure solution method	SAD
RMSD bond length	0.007 *
RMSD bond angle	21.300 *
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	2.690
High resolution limit [Å]	2.600	2.600
Rmerge	0.047 *	0.508 *
Number of reflections	83954	8294 *
<I/σ(I)>	31.6	2.3
Completeness [%]	98.1	98.1
Redundancy	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.8	25 *	100 mM HEPES pH 6.8, 1.2-1.35 M Sodium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	HEPES	100 (mM)	pH6.8
3	1	reservoir	sodium acetate	1.2-1.35 (M)