9EQF

Crystal structure of the L-arginine hydroxylase VioC MeHis316, bound to Fe(II), L-arginine, and succinate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-10-16
Detector	DECTRIS EIGER2 S 16M
Wavelength(s)	0.976
Spacegroup name	C 1 2 1
Unit cell lengths	81.145, 67.107, 62.945
Unit cell angles	90.00, 109.22, 90.00

Refinement procedure

Resolution	38.480 - 1.600
R-factor	0.1593
Rwork	0.158
R-free	0.18680
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.810
Data reduction software	DIALS
Data scaling software	DIALS
Phasing software	PHENIX
Refinement software	PHENIX (1.21_5207)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.480	1.640
High resolution limit [Å]	1.600	1.600
Number of reflections	41962	2681
<I/σ(I)>	15.47	1.86
Completeness [%]	99.6	96.09
Redundancy	6.6
CC(1/2)	0.999	0.922

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		277	final concentration of 10 mg ml-1 protein, in 20 mM HEPES buffer pH 7.5 containing 0.4 mM ammonium iron(II) sulphate hexahydrate, 2 mM L-arginine and 2 mM succinate, mixed 1:1 volume with 0.02 M magnesium chloride hexahydrate, 0.1 M HEPES, pH 7.5, containing 22 % (w/v) poly(acrylic acid sodium salt) 5100