6X0H

Structure of oxidized SidA ornithine hydroxylase with the FAD in the "out" conformation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-02-25
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.979180
Spacegroup name	P 1 21 1
Unit cell lengths	76.765, 156.937, 88.651
Unit cell angles	90.00, 110.38, 90.00

Refinement procedure

Resolution	65.411 - 2.087
R-factor	0.1849
Rwork	0.182
R-free	0.23220
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4b63
RMSD bond length	0.007
RMSD bond angle	0.919
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]	156.940	156.940	2.120
High resolution limit [Å]	2.087	11.430	2.090
Rmerge	0.110	0.025	0.858
Rmeas	0.142	0.032	1.113
Rpim	0.088	0.020	0.702
Total number of observations		1659	10926
Number of reflections	114542	696	5054
<I/σ(I)>	6	17.6	1
Completeness [%]	98.4	95.4	87.4
Redundancy	2.3	2.4	2.2
CC(1/2)	0.991	0.997	0.416

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	293	Enzyme stock solution: 8-10 mg/mL SidA 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