7C5D
Crystal structure of TRF2 TRFH domain in complex with a MCPH1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-03-17 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9785 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.737, 74.941, 98.418 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.890 - 2.151 |
| R-factor | 0.1911 |
| Rwork | 0.189 |
| R-free | 0.23480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h6p |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.645 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.190 |
| High resolution limit [Å] | 2.150 | 5.830 | 2.150 |
| Rmerge | 0.077 | 0.024 | 0.599 |
| Rmeas | 0.080 | 0.025 | 0.626 |
| Rpim | 0.022 | 0.007 | 0.181 |
| Total number of observations | 326030 | ||
| Number of reflections | 25033 | 1392 | 1236 |
| <I/σ(I)> | 4.4 | ||
| Completeness [%] | 99.9 | 99.9 | 99.6 |
| Redundancy | 13 | 11.7 | 11.8 |
| CC(1/2) | 1.000 | 0.921 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 293 | 30% PEG400, 100 mM CHES-NaOH, pH 9.5 |
