3ZE8

3D structure of the Ni-Fe-Se hydrogenase from D. vulgaris Hildenborough in the reduced state at 1.95 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	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	72.227, 97.632, 103.348
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.140 - 1.801
R-factor	0.1368
Rwork	0.135
R-free	0.16580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2wpn
RMSD bond length	0.008
RMSD bond angle	1.104
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX ((PHENIX.REFINE: 1.8.1_1168))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.100	1.910
High resolution limit [Å]	1.800	1.800
Rmerge	0.070	0.340
Number of reflections	64222
<I/σ(I)>	16.2	4.1
Completeness [%]	94.0	96.3
Redundancy	3.9	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	CRYSTALS WERE GROWN USING THE SITTING-DROP VAPOR DIFFUSION METHOD AT 20C 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.