2RHX

Crystal structure of the 3-MBT repeats from human L3MBTL1 bound to dimethyl-lysine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	CCD
Collection date	2007-02-26
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9792
Spacegroup name	P 21 21 2
Unit cell lengths	86.272, 93.104, 59.286
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.100
Rwork	0.196
R-free	0.22600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1oz2
RMSD bond length	0.006
RMSD bond angle	1.430
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	2.170
High resolution limit [Å]	2.100	2.100
Rmerge	0.082	0.572
Number of reflections	28356
<I/σ(I)>	20.3	2.7
Completeness [%]	99.4	99.9
Redundancy	3.8	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	Crystals of the Kme2-L3MBTL1(197-526) complex were generated by pre-incubating L3MBTL1 (17MG/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 (0.1 M bis-Tris, pH 6.5, 15% PEG MME 5000, 0.15 M ammonium sulfate, and 10 mM DTT)., VAPOR DIFFUSION, HANGING DROP, temperature 293K