7LTF
Structure of the alpha-N-methyltransferase (SonM mutant Y58F) and RiPP precursor (SonA) heteromeric complex (no cofactor)
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) | 1.033167 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.370, 108.500, 58.950 |
Unit cell angles | 90.00, 94.13, 90.00 |
Refinement procedure
Resolution | 58.800 - 2.200 |
Rwork | 0.226 |
R-free | 0.23760 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5n0p |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (v5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 58.800 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 33041 | 4031 |
<I/σ(I)> | 15.48 | |
Completeness [%] | 99.1 | |
Redundancy | 4.61 | |
CC(1/2) | 0.991 | 0.978 |
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 |