8YE8
Crystal structure of mouse BAHCC1 TTD domain in complex with H4K20me1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-10-08 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 57.695, 65.286, 78.670 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.525 - 1.900 |
| R-factor | 0.191012499984 |
| Rwork | 0.187 |
| R-free | 0.23774 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | in-house Se-SAD model |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.152 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692+SVN) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.071 | 0.069 |
| Number of reflections | 24054 | 1835 |
| <I/σ(I)> | 46 | |
| Completeness [%] | 99.9 | |
| Redundancy | 12.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 100 mM MES, pH 6.5, 10 mM Li2SO4, 8% PEG20000 and 3 mM H4K20me |
