8Q5X

MgADP-bound Fe protein of the molybdenum nitrogenase from Methanococcus maripaludis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06DA
Synchrotron site	SLS
Beamline	X06DA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-12-10
Detector	DECTRIS PILATUS 2M-F
Wavelength(s)	0.99999
Spacegroup name	P 1 21 1
Unit cell lengths	68.546, 111.094, 78.820
Unit cell angles	90.00, 90.01, 90.00

Refinement procedure

Resolution	46.890 - 1.700
R-factor	0.1618
Rwork	0.160
R-free	0.18590
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	0.913
Data reduction software	autoPROC
Data scaling software	autoPROC
Phasing software	PHASER
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	78.820	1.860
High resolution limit [Å]	1.700	1.700
Rmerge	0.219	1.232
Rmeas	0.237	1.336
Rpim	0.090	0.511
Number of reflections	94344	4718
<I/σ(I)>	7.5	1.6
Completeness [%]	94.2	57.6
Redundancy	6.9	6.6
CC(1/2)	0.992	0.468

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293.15	The purified protein was crystallised at a final concentration of 13 mg/ml with 2 mM ATP and 2 mM MgCl2 by spotting 0.7 ul of crystallisation solution with 0.7 ul of protein sample. Crystallisation was done anaerobically in a Coy tent containing N2/H2 (97:3%) atmosphere. The screening was done at 20 degrees Celsius on 96-Well MRC 2-drop polystyrene (SWISSCI) plates containing 90 ul of crystallisation solution. The crystallisation solution in which crystals were obtained contained 20 % w/v polyethylene glycol 3000, 100 mM Tris pH 7.0 and 200 mM calcium acetate. The crystal was soaked in the crystallisation solution supplemented with 20% glycerol prior to freezing in liquid nitrogen.