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