6OGN
Crystal structure of mouse protein arginine methyltransferase 7 in complex with SGC8158 chemical probe
Replaces: 6NPGExperimental 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 | 2019-02-20 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 97.813, 97.813, 169.539 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.030 - 2.400 |
| R-factor | 0.2111 |
| Rwork | 0.208 |
| R-free | 0.26122 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 4c4a |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.365 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 6.510 | 2.400 |
| Rmerge | 0.114 | 0.072 | 1.172 |
| Rmeas | 0.118 | 0.075 | 1.223 |
| Rpim | 0.033 | 0.022 | 0.346 |
| Number of reflections | 33363 | 1830 | 1622 |
| <I/σ(I)> | 9.5 | ||
| Completeness [%] | 99.7 | 97.4 | 100 |
| Redundancy | 12.9 | 12 | 12.2 |
| CC(1/2) | 0.986 | 0.689 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.4 | 293 | 20% PEG3350, 0.04 M citric acid, 0.06 M Bis-Tris propane, pH 6.4 |






