9QR3

Methyl-coenzyme M reductase of an ANME-2c from a microbial enrichment

This is a non-PDB format compatible entry.

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	2022-04-28
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97856
Spacegroup name	P 1 21 1
Unit cell lengths	156.867, 157.456, 215.422
Unit cell angles	90.00, 90.34, 90.00

Refinement procedure

Resolution	98.930 - 1.340
R-factor	0.1142
Rwork	0.112
R-free	0.14710
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.247
Data reduction software	autoPROC
Data scaling software	STARANISO
Phasing software	PHASER
Refinement software	PHENIX ((1.21.2_5419: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	127.160	1.500
High resolution limit [Å]	1.340	1.340
Rmerge	0.168	1.671
Rmeas	0.183	1.829
Rpim	0.073	0.737
Number of reflections	1527343	76367
<I/σ(I)>	6.6	1.6
Completeness [%]	96.2	66.6
Redundancy	6.3	6
CC(1/2)	0.991	0.560

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293.15	2 ul protein at 24.6 g/l in 25 mM Tris/HCl pH 7.6, 10 % v/v glycerol, and 2 mM dithiothreitol was mixed with 2 ul crystallisation solution (30 % v/v 2-Methyl-2,4-pentanediol, 100 mM Tris pH 8.5, 500 mM NaCl, and 8% polyethylene glycol 8000) on a Junior Clover plate (Jena Bioscience). The reservoir contained 90 ul of crystallisation solution.