7JVK

Structure of the M101A variant of the SidA ornithine hydroxylase with the FAD in the "out" conformation

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	2017-07-21
Detector	RDI CMOS_8M
Wavelength(s)	1.0000
Spacegroup name	P 1 21 1
Unit cell lengths	76.437, 155.275, 88.271
Unit cell angles	90.00, 110.33, 90.00

Refinement procedure

Resolution	56.630 - 2.200
R-factor	0.1952
Rwork	0.195
R-free	0.22970
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	6x0h
RMSD bond length	0.007
RMSD bond angle	0.942
Data reduction software	XDS
Data scaling software	Aimless (0.7.4)
Phasing software	PHENIX
Refinement software	PHENIX (1.18)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	61.440	61.440	2.240
High resolution limit [Å]	2.200	12.050	2.200
Rmerge	0.108	0.024	1.235
Rmeas	0.128	0.029	1.514
Rpim	0.067	0.016	0.859
Total number of observations	340416	2167	12230
Number of reflections	96363	610	4315
<I/σ(I)>	10.8	44.3	0.9
Completeness [%]	98.7	97.9	89.2
Redundancy	3.5	3.6	2.8
CC(1/2)	0.995	0.990	0.484

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	Enzyme stock solution: 8-10 mg/ml SidA (M101A) 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. Drop ratio: 2 enzyme to 1 reservoir