8B1N

Crystal structure of TrmD-Tm1570 from Calditerrivibrio nitroreducens in complex with S-adenosyl-L-methionine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-04-30
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.9184
Spacegroup name	P 21 21 2
Unit cell lengths	96.780, 199.560, 56.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.920 - 2.000
R-factor	0.1703
Rwork	0.169
R-free	0.20880
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5wyr 3dcm
RMSD bond length	0.006
RMSD bond angle	0.824
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.300	2.120
High resolution limit [Å]	2.000	2.000
Rmeas	0.138	1.523
Number of reflections	75191	11921
<I/σ(I)>	13.68	1.43
Completeness [%]	99.9	99.4
Redundancy	8.81	8.69
CC(1/2)	0.999	0.616

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293.15	Protein sample: 5.7 mg/mL TrmD-Tm1570 in 50 mM HEPES buffer pH 7.4, 300 mM NaCl, 5% glycerol, with addition of 3 mM SAM, 0.1% DDM and 3000x diluted seeds stock. Reservoir solution: 0.2 M MgCl2, 0.1 M Tris pH 7.0, 10% PEG 8000.