2RHY
Crystal structure of the 3-MBT repeats from human L3MBTL1 bound to monomethyl-lysine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-06-15 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 85.460, 92.607, 58.674 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.900 |
Rwork | 0.210 |
R-free | 0.23000 |
Structure solution method | Molrep |
Starting model (for MR) | 1oz2 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.440 |
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 | 0.076 | 0.485 |
Number of reflections | 37422 | |
<I/σ(I)> | 24.7 | 3.7 |
Completeness [%] | 99.8 | 99.3 |
Redundancy | 5.7 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | Crystals was generated by pre-incubating the L3MBTL1 (12MG/ML IN 50MM KCL, 25MM TRIS-HCL PH 8.0, 1MM DTT) with a five-fold molar excess of monomethyl-lysine amino acid. Drops were prepared by mixing equal volumes of the complex with reservoir solution (7.5% PEG10K, 0.1 M Tris-maleate pH 6.5, 0.1 M ammonium sulfate), VAPOR DIFFUSION, HANGING DROP, temperature 293K |