6X0J

Structure of reduced SidA ornithine hydroxylase with the FAD "in" and complexed with NADP and L-ornithine

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	85.208, 153.015, 91.114
Unit cell angles	90.00, 110.91, 90.00

Refinement procedure

Resolution	56.899 - 2.335
R-factor	0.1866
Rwork	0.183
R-free	0.24910
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4b63
RMSD bond length	0.007
RMSD bond angle	1.020
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]	153.010	153.010	2.380
High resolution limit [Å]	2.335	12.790	2.340
Rmerge	0.198	0.025	1.372
Rmeas	0.227	0.029	1.637
Rpim	0.111	0.014	0.874
Total number of observations		2369	9559
Number of reflections	90888	590	3292
<I/σ(I)>	8.9	41.9	0.8
Completeness [%]	98.5	98.9	71.9
Redundancy	4.1	4	2.9
CC(1/2)	0.984	0.999	0.352

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	293	Enzyme stock solution: 8-10 mg/mL SidA, 1 mM NADP, and 15 mM L-Orn 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, 100 mM NADPH and 15 mM L-Orn