3OMC
Structure of human SND1 extended tudor domain in complex with the symmetrically dimethylated arginine PIWIL1 peptide R4me2s
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2010-06-11 |
| Detector | RIGAKU RAXIS HTC |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 35.622, 75.834, 80.177 |
| Unit cell angles | 90.00, 90.37, 90.00 |
Refinement procedure
| Resolution | 25.050 - 1.770 |
| R-factor | 0.1803 |
| Rwork | 0.179 |
| R-free | 0.21310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o4x |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.175 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.6.0081) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.770 | 3.810 | 1.770 |
| Rmerge | 0.040 | 0.018 | 0.282 |
| Number of reflections | 41508 | ||
| <I/σ(I)> | 18.8 | ||
| Completeness [%] | 99.6 | 99.6 | 98 |
| Redundancy | 3.6 | 3.7 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 30% PEG1500, 1:500 V8 PROTEASE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K |






