4RQI
Structure of TRF2/RAP1 secondary interaction binding site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-10-14 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.98 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.790, 104.850, 85.310 |
Unit cell angles | 90.00, 94.39, 90.00 |
Refinement procedure
Resolution | 47.020 - 2.441 |
R-factor | 0.1996 |
Rwork | 0.197 |
R-free | 0.24060 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.976 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.020 | 2.630 |
High resolution limit [Å] | 2.440 | 2.440 |
Rmerge | 0.068 | 0.664 |
Number of reflections | 33979 | |
<I/σ(I)> | 2.26 | |
Completeness [%] | 98.0 | 79.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | PEGmme 550, Hepes buffer, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |