3OMG
Structure of human SND1 extended tudor domain in complex with the symmetrically dimethylated arginine PIWIL1 peptide R14me2s
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-06-30 |
Detector | RIGAKU SATURN A200 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 35.721, 75.804, 80.073 |
Unit cell angles | 90.00, 90.36, 90.00 |
Refinement procedure
Resolution | 80.070 - 1.850 |
R-factor | 0.1943 |
Rwork | 0.192 |
R-free | 0.23860 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2o4x |
RMSD bond length | 0.011 |
RMSD bond angle | 1.200 |
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] | 80.070 | 50.000 | 1.920 |
High resolution limit [Å] | 1.850 | 3.990 | 1.850 |
Rmerge | 0.084 | 0.037 | 0.448 |
Number of reflections | 35716 | ||
<I/σ(I)> | 9.9 | ||
Completeness [%] | 97.9 | 99.7 | 85.9 |
Redundancy | 5.2 | 5.5 | 3.9 |
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 |