8T1S
Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAH)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-03-03 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.390, 108.730, 59.140 |
| Unit cell angles | 90.00, 93.66, 90.00 |
Refinement procedure
| Resolution | 52.280 - 2.000 |
| R-factor | 0.2045 |
| Rwork | 0.203 |
| R-free | 0.23814 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.553 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.280 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmeas | 0.111 | 0.582 |
| Number of reflections | 44465 | 6044 |
| <I/σ(I)> | 10.89 | |
| Completeness [%] | 99.7 | |
| Redundancy | 5.41 | |
| CC(1/2) | 0.997 | 1.000 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 292 | 240 mM sodium malonate pH 5-5.5, 8-12% PEG 3350 at a 1-1 or 2-1 ratio of protein to mother liquor. Protein concentration is 20mg/mL. |






