4U9B

Crystal structure of an H-NOX protein from S. oneidensis in the Fe(II)NO ligation state

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.1
Synchrotron site	ALS
Beamline	8.2.1
Temperature [K]	100
Detector technology	CCD
Collection date	2012-07-07
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.11
Spacegroup name	P 21 21 2
Unit cell lengths	67.636, 86.716, 33.822
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.818 - 1.650
R-factor	0.1693
Rwork	0.168
R-free	0.20270
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4u99
RMSD bond length	0.019
RMSD bond angle	0.864
Refinement software	PHENIX ((phenix.refine: 1.9_1692))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.818	1.740
High resolution limit [Å]	1.650	1.650
Rmerge	0.029	0.487
Number of reflections	45550
<I/σ(I)>	14.4	1.7
Completeness [%]	98.5	99.5
Redundancy	3.9	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Obtained by equilibrating a 2 or 4 uL drop of 1:1 protein: reservoir against 700 uL reservoir containing 0.7 M NaH2PO4, 0.9 M K2HPO4. Cryoprotection was achieved by carefully adding equal drop volume of mother liquor containing 50% glycerol. Crystals were then transferred into mother liquor containing 30% glycerol and flash frozen in liquid nitrogen. All crystal growth and manipulation was performed anaerobically.