6X0I

Structure of oxidized SidA ornithine hydroxylase with the FAD "in" and complexed with NADP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CMOS
Collection date	2016-04-27
Detector	RDI CMOS_8M
Wavelength(s)	1.00004
Spacegroup name	P 1 21 1
Unit cell lengths	80.507, 154.868, 90.483
Unit cell angles	90.00, 109.25, 90.00

Refinement procedure

Resolution	63.210 - 1.950
R-factor	0.1703
Rwork	0.168
R-free	0.21100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4b63
RMSD bond length	0.006
RMSD bond angle	0.869
Data reduction software	XDS
Data scaling software	Aimless (0.5.23)
Phasing software	PHASER
Refinement software	PHENIX (1.14)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	63.210	63.210	1.980
High resolution limit [Å]	1.950	10.680	1.950
Rmerge	0.092	0.022	0.790
Rmeas	0.108	0.026	0.947
Rpim	0.056	0.014	0.516
Total number of observations	544409	3440	24487
Number of reflections	151085	954	7458
<I/σ(I)>	12.1	46.4	1.5
Completeness [%]	99.5	98.2	99
Redundancy	3.6	3.6	3.3
CC(1/2)	0.997	0.999	0.523

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	293	Enzyme stock solution: 8-10 mg/mL SidA and 1 mM NADP in 25 mM HEPES (pH 7.5) and 100 mM NaCl. Crystallization reservoir: 17-21 % PEG-3350, 0.1 M HEPES (pH 7.5), 0.1 M calcium acetate. Cryo-buffer: 15 % PEG-200, 20 % PEG 3350, 0.1 M HEPES (pH 7.5), 0.1 M calcium acetate