8DS8
Crystal structure of human TNRC18 BAH domain in complex with H3K9me3 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-07-27 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 73.804, 120.828, 46.632 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.480 - 1.840 |
| R-factor | 0.2043 |
| Rwork | 0.203 |
| R-free | 0.23490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4dov |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.974 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.920 |
| High resolution limit [Å] | 1.840 | 3.990 | 1.840 |
| Rmerge | 0.124 | 0.053 | 1.210 |
| Rmeas | 0.139 | 0.059 | 1.380 |
| Rpim | 0.061 | 0.025 | 0.649 |
| Number of reflections | 36692 | 3909 | 3584 |
| <I/σ(I)> | 5.2 | ||
| Completeness [%] | 99.5 | 99.2 | 99.7 |
| Redundancy | 5.2 | 5.5 | 4.5 |
| CC(1/2) | 0.997 | 0.590 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 0.1 M Sodium Cacodylate, pH 6.5, 0.2 M Magnesium Acetate, 16-20% PEG 8000 |






