7LTR
Structure of the heteromeric complex between the alpha-N-methyltransferase (SonM) and a truncated construct of the RiPP precursor (SonA) (with SAM)
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 1 21 1 |
| Unit cell lengths | 72.240, 112.860, 85.870 |
| Unit cell angles | 90.00, 97.82, 90.00 |
Refinement procedure
| Resolution | 56.430 - 1.750 |
| R-factor | 0.1889 |
| Rwork | 0.187 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5n0p |
| RMSD bond length | 0.002 |
| RMSD bond angle | 1.123 |
| 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] | 56.430 | 1.850 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Number of reflections | 134823 | 20453 |
| <I/σ(I)> | 24.88 | |
| Completeness [%] | 98.3 | |
| Redundancy | 4.29 | |
| CC(1/2) | 0.983 | 0.974 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | proteins at 20 mg/mL and crystallized in 100 mM Bis-Tris at pH 5.5 with 100 mM ammonium acetate and 4-7% PEG 10000 |
