8QQ7

Structure of SpNOX: a Bacterial NADPH oxidase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-05-11
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.966
Spacegroup name	P 64 2 2
Unit cell lengths	145.967, 145.967, 153.619
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.820 - 3.620
R-factor	0.2642
Rwork	0.262
R-free	0.32003
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	model from PROMALS3D and I-TASSER
RMSD bond length	0.006
RMSD bond angle	1.727
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.820	3.950
High resolution limit [Å]	3.620	3.620
Rmerge	0.072	2.000
Rmeas	0.074
Rpim	0.017	0.465
Number of reflections	5508	275
<I/σ(I)>	19.6	1.5
Completeness [%]	90.9	85.4
Redundancy	20	20

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	Protein: 4.04 mg/ml in 50 mM Tris pH 7, 300 mM NaCl, 0.025 mM MNG3, 0.01 mM FAD. Crystallization condition: 30.5% PEG 300, 0.15 M Li2SO4, 0.15 M NaCl and 0.1 M MES pH6. Drop: 6 uL of protein + 6 uL of well.