7LTE
Structure of the alpha-N-methyltransferase (SonM) 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) | 1.033167 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.460, 108.660, 59.090 |
Unit cell angles | 90.00, 94.10, 90.00 |
Refinement procedure
Resolution | 58.940 - 2.000 |
R-factor | 0.2137 |
Rwork | 0.212 |
R-free | 0.24440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5n0p |
RMSD bond length | 0.012 |
RMSD bond angle | 1.408 |
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] | 58.940 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 42332 | 6106 |
<I/σ(I)> | 14.49 | |
Completeness [%] | 94.6 | |
Redundancy | 3.18 | |
CC(1/2) | 0.997 | 0.991 |
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 |