5H5D
The crystal structure of the yeast arginine methyltransferase SFM1 complexed with MTA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-06-06 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.527, 57.770, 43.153 |
| Unit cell angles | 90.00, 106.46, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.700 |
| R-factor | 0.23216 |
| Rwork | 0.230 |
| R-free | 0.28217 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5c77 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.435 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.100 | 0.314 |
| Number of reflections | 5087 | |
| <I/σ(I)> | 11.5 | 1.9 |
| Completeness [%] | 95.4 | 88.1 |
| Redundancy | 2.6 | 2 |
| CC(1/2) | 0.816 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 0.2 M NaCl, 0.1 M Tris-HCl (pH 8.5), 38% PEG 3350 |
