6CO2
Structure of an engineered protein (NUDT16TI) 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 43 21 2 |
| Unit cell lengths | 73.689, 73.689, 276.448 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.225 - 2.490 |
| R-factor | 0.2227 |
| Rwork | 0.220 |
| R-free | 0.26970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2g3r 2xsq |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.430 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.225 | 2.579 |
| High resolution limit [Å] | 2.490 | 2.490 |
| Rmerge | 0.127 | 1.110 |
| Number of reflections | 27761 | 2689 |
| <I/σ(I)> | 20.47 | 2.16 |
| Completeness [%] | 99.9 | 99.63 |
| Redundancy | 42.9 | 30.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 0.1 M sodium citrate tribasic dehydrate, pH 5.6, 0.2 M ammonium acetate, 10% PEG 4,000 |
