2RJC
Crystal structure of L3MBTL1 protein in complex with MES
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ DW |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-12-10 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.54000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 63.548, 108.784, 90.348 |
Unit cell angles | 90.00, 90.91, 90.00 |
Refinement procedure
Resolution | 90.170 - 2.000 |
R-factor | 0.19718 |
Rwork | 0.195 |
R-free | 0.24127 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pqw |
RMSD bond length | 0.020 |
RMSD bond angle | 1.679 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 90.170 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.088 |
Number of reflections | 82054 |
Completeness [%] | 99.9 |
Redundancy | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.1 | 300 | 4% PEG 4000, 0.1 M Sodium acetate, 0.1 M MES pH 5.1, VAPOR DIFFUSION, HANGING DROP, temperature 300K |