2RHU

Crystal structure of the 3-MBT repeats from human L3MBTL1 bound to dimethyl-lysine and in chimera with histone H3.3(28-34)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2007-06-09
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.54
Spacegroup name	P 21 21 2
Unit cell lengths	85.166, 94.023, 59.187
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.900
Rwork	0.194
R-free	0.21500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1oz2
RMSD bond length	0.007
RMSD bond angle	1.490
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.068	0.414
Number of reflections	38237
<I/σ(I)>	26.8	5
Completeness [%]	100.0	100
Redundancy	6.4	6.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	6.5	293	Crystals was generated by pre-incubating the L3MBTL1-H3.3(28-34) (18MG/ML IN 50MM KCL, 25MM TRIS-HCL PH 8.0, 1MM DTT) with a five-fold molar excess of dimethyl-lysine amino acid. Drops were prepared by mixing equal volumes of the complex with reservoir solution (5% PEG10K, 0.1 M Tris-maleate pH 6.5, 0.1 M ammonium sulfate), VAPOR DIFFUSION, temperature 293K