1KW0

Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-04-08
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.8000
Spacegroup name	C 2 2 21
Unit cell lengths	65.172, 106.741, 123.440
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.500
Rwork	0.220
R-free	0.26700
Structure solution method	adopting entry 1PAH phases
Starting model (for MR)	1pah
RMSD bond length	0.007
RMSD bond angle	21.900 *
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000	2.640
High resolution limit [Å]	2.500	2.500
Rmerge	0.092	0.377
Total number of observations	59237 *
Number of reflections	14178	2071 *
<I/σ(I)>	7.1	2.1
Completeness [%]	94.4	95.2
Redundancy	4.2	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.8	277	20% PEG 2000, 10% ethylene glycol 0.12M Na-Hepes pH 6.8, 30mM Na-dithionite, 10mM BH4, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop		5 (mM)
2	1	drop	sodium dithionite	15 (mM)