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