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 |