3ZE6

3D structure of the Ni-Fe-Se hydrogenase from D. vulgaris Hildenborough in the as-isolated oxidized state at 1.50 Angstroms

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06DA
Synchrotron site	SLS
Beamline	X06DA
Temperature [K]	100
Detector technology	CCD
Collection date	2009-07-18
Detector	MARMOSAIC 225 mm CCD
Spacegroup name	P 21 21 21
Unit cell lengths	72.170, 97.350, 102.970
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.512 - 1.500
R-factor	0.1359
Rwork	0.135
R-free	0.15430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2wpn
RMSD bond length	0.012
RMSD bond angle	1.476
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.500	1.540
High resolution limit [Å]	1.500	1.500
Rmerge	0.090	0.590
Number of reflections	114933
<I/σ(I)>	17.5	3
Completeness [%]	98.6	88.5
Redundancy	7.2	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5		CRYSTALS WERE GROWN BY THE SITTING DROP VAPOR DIFFUSION METHOD, BY MIXING 1.5 UL OF RESERVOIR SOLUTION CONTAINING 20% POLYETHYLENE GLYCOL (PEG) 1500, 0.1 M TRIS-HCL, PH 8.5 AND AN EQUAL VOLUME OF A SOLUTION COMPOSED OF 10 MG/ML OF PROTEIN IN 10 MM TRIS-HCL BUFFER AT PH 7.6.