7NKG

Methyl-coenzyme M reductase from Methermicoccus shengliensis at 1.6-A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 1
Synchrotron site	SOLEIL
Beamline	PROXIMA 1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-11-23
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97856
Spacegroup name	P 21 21 21
Unit cell lengths	132.615, 148.177, 235.415
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.360 - 1.600
R-factor	0.1734
Rwork	0.172
R-free	0.19040
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e6y
RMSD bond length	0.007
RMSD bond angle	0.950
Data reduction software	XDS
Data scaling software	SCALA (3.3.22)
Phasing software	PHASER (2.8.2)
Refinement software	BUSTER (2.10.3 (19-MAR-2020))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.410	1.690
High resolution limit [Å]	1.600	1.600
Rmerge	0.091	1.216
Rmeas	0.105	1.388
Rpim	0.051	0.661
Number of reflections	602614	87124
<I/σ(I)>	8.3	1
Completeness [%]	99.7	99.3
Redundancy	4.2	4.3
CC(1/2)	0.997	0.356

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	291.15	The protein sample was at 47 g/l in 25 mM Tris/HCl pH 7.6, 10% v/v glycerol and 2 mM dithiothreitol. MCR crystals were obtained aerobically by using the sitting drop method on 96-Well MRC 2-Drop Crystallization Plates in polystyrene (SWISSCI). The crystallization reservoir contained 90 ul of mother liquor; the crystallization drop contained a mixture of 0.6 ul protein sample and 0.6 ul of crystallization solution. The crystallization solution contained 25% w/v polyethylene glycol 3350, 100 mM Bis-Tris pH 5.5 and 200 mM lithium sulfate.