7LTC

Structure of the alpha-N-methyltransferase (SonM) 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	52.510, 108.620, 59.020
Unit cell angles	90.00, 94.00, 90.00

Refinement procedure

Resolution	47.180 - 2.000
Rwork	0.205
R-free	0.23310
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]	47.180	2.100
High resolution limit [Å]	2.000	2.000
Number of reflections	43871	6015
<I/σ(I)>	15.53
Completeness [%]	98.4
Redundancy	4.5
CC(1/2)	0.998	0.988

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