5V22
Crystal structure of human SETD2 SET-domain in complex with H3K36M peptide and SAH
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 | CCD |
| Collection date | 2016-06-23 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.287, 77.196, 76.527 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.400 |
| R-factor | 0.1982 |
| Rwork | 0.195 |
| R-free | 0.25700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4h12 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.797 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.7_650) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.085 | 0.429 |
| Number of reflections | 14491 | 1421 |
| <I/σ(I)> | 18.8 | 3.7 |
| Completeness [%] | 99.7 | |
| Redundancy | 5.4 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1 M KSCN, 24% (v/v) PEG 2000 MME |
