7LTS
Structure of the alpha-N-methyltransferase (SonM mutant R67A) and RiPP precursor (SonA) heteromeric complex (with SAH)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-03-12 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.991840 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 80.950, 80.950, 236.470 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 76.590 - 2.320 |
| R-factor | 0.2001 |
| Rwork | 0.198 |
| R-free | 0.24780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5n0p |
| RMSD bond length | 0.002 |
| RMSD bond angle | 1.160 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0266) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 76.590 | 2.450 |
| High resolution limit [Å] | 2.320 | 2.320 |
| Number of reflections | 35110 | 5161 |
| <I/σ(I)> | 19.16 | |
| Completeness [%] | 99.9 | |
| Redundancy | 19.16 | |
| CC(1/2) | 0.999 | 0.846 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | Proteins were concentrated at 20 mg/mL and crystallized at pH ranging between 5.5-7 and using PEG 3,350 (0-20%) as precipitant |
