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 |