6W6D
Crystal Structure of Human Protein arginine N-methyltransferase 6 (PRMT6) in complex with SGC6870 inhibitor
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 | 2019-07-20 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | I 41 |
| Unit cell lengths | 94.603, 94.603, 108.094 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.350 - 1.910 |
| R-factor | 0.1822 |
| Rwork | 0.181 |
| R-free | 0.20940 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 5wcf |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.446 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.940 |
| High resolution limit [Å] | 1.910 | 5.180 | 1.910 |
| Rmerge | 0.076 | 0.052 | 0.976 |
| Rmeas | 0.083 | 0.056 | 1.068 |
| Rpim | 0.033 | 0.022 | 0.430 |
| Total number of observations | 230004 | ||
| Number of reflections | 36823 | 1891 | 1831 |
| <I/σ(I)> | 11.6 | ||
| Completeness [%] | 99.8 | 99.9 | 99.9 |
| Redundancy | 6.2 | 6.2 | 6.1 |
| CC(1/2) | 0.997 | 0.586 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 291 | 12% (w/v) PEG3350, 4% (v/v) Tascimate TM pH 7.0 |
