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 |
