9CH7
Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-Y62A) heteromeric complex (bound to SAH - structure 1)
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 | 2023-02-26 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.0332 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 72.170, 111.480, 85.540 |
Unit cell angles | 90.00, 96.83, 90.00 |
Refinement procedure
Resolution | 60.280 - 2.200 |
R-factor | 0.18215 |
Rwork | 0.180 |
R-free | 0.21898 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.001 |
RMSD bond angle | 0.752 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.280 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmeas | 0.073 | 0.761 |
Number of reflections | 68051 | 8440 |
<I/σ(I)> | 14.43 | |
Completeness [%] | 99.8 | |
Redundancy | 5.45 | |
CC(1/2) | 0.999 | 0.815 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 240 mM sodium malonate pH 5.5 and 22% PEG 3350 |