6AGO
Crystal structure of MRG15-ASH1L Histone methyltransferase complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE AR-NE3A |
| Synchrotron site | Photon Factory |
| Beamline | AR-NE3A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-02-18 |
| Detector | DECTRIS PILATUS 2M-F |
| Wavelength(s) | 1 |
| Spacegroup name | P 31 1 2 |
| Unit cell lengths | 115.757, 115.757, 209.282 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.917 - 3.103 |
| R-factor | 0.2235 |
| Rwork | 0.220 |
| R-free | 0.27230 |
| Structure solution method | SAD |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.150 |
| High resolution limit [Å] | 3.100 | 8.400 | 3.100 |
| Rmerge | 0.064 | 0.033 | 0.736 |
| Rmeas | 0.071 | 0.037 | 0.830 |
| Rpim | 0.030 | 0.016 | 0.373 |
| Total number of observations | 147885 | ||
| Number of reflections | 29386 | 1554 | 1461 |
| <I/σ(I)> | 8 | ||
| Completeness [%] | 99.9 | 99.6 | 99.9 |
| Redundancy | 5 | 4.8 | 4.6 |
| CC(1/2) | 0.998 | 0.814 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 295 | Ammonium Acetate |






