6CO1
Structure of human TIRR in complex with 53BP1 Tudor domains
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-10-15 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9791 |
| Spacegroup name | P 1 |
| Unit cell lengths | 61.840, 77.030, 77.240 |
| Unit cell angles | 85.24, 86.07, 86.09 |
Refinement procedure
| Resolution | 38.310 - 2.179 |
| R-factor | 0.1669 |
| Rwork | 0.164 |
| R-free | 0.20330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2g3r 3kvh |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.460 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.627 | 2.257 |
| High resolution limit [Å] | 2.179 | 2.179 |
| Rmerge | 0.133 | 0.862 |
| Number of reflections | 73587 | 7203 |
| <I/σ(I)> | 17.9 | 4.1 |
| Completeness [%] | 99.6 | 97.72 |
| Redundancy | 14.4 | 12.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 0.1 M MES, pH 5.5, 0.2 M calcium acetate, 7% isopropanol |
