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 |