6N1K

Full-length human phenylalanine hydroxylase (PAH) in the resting state

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-1
Synchrotron site	NSLS-II
Beamline	17-ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-06-29
Detector	DECTRIS EIGER X 9M
Wavelength(s)	1.008
Spacegroup name	P 1 21 1
Unit cell lengths	72.437, 202.640, 72.574
Unit cell angles	90.00, 90.30, 90.00

Refinement procedure

Resolution	36.287 - 3.057
R-factor	0.2076
Rwork	0.203
R-free	0.23800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1j8u
RMSD bond length	0.002
RMSD bond angle	0.500
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHENIX (1.12rc1_2807)
Refinement software	PHENIX ((1.12rc1_2807: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.000	3.166
High resolution limit [Å]	3.050	3.057
Rmerge	0.078
Rmeas	0.091
Number of reflections	39316	3885
<I/σ(I)>	11.45	1.67
Completeness [%]	99.5	98.16
Redundancy	3.9	3.9
CC(1/2)	0.998	0.630

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	295	hPAH C29S was obtained from of the 6His-SUMO fusion using a sodium phosphate buffer. Crystals were grown from C29S (16 mg/mL) in 2 mM Tris-HCl pH 7.4, mixed with reservoir solutions in a protein:reservoir ratio equal to 1:1.25 and equilibrated using hanging drop vapor diffusion. The 1 mL reservoir solution initially contained 16% PEG 3350, 100 mM bis-tris-propane pH 7.5 and 200 mM sodium sulfate. Crystals appeared at 295K within one day in the dark.