1PAH

HUMAN PHENYLALANINE HYDROXYLASE DIMER, RESIDUES 117-424

Experimental procedure

Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-05
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	66.600, 108.400, 125.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.176
Rwork	0.176
R-free	0.21800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1toh
RMSD bond length	0.090
RMSD bond angle	25.070 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.048	0.390
Total number of observations	18331 *
Number of reflections	30932
<I/σ(I)>	20.7	20
Completeness [%]	99.7	99.1
Redundancy	5.9	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.8		Erlandsen, H., (1997) FEBS Lett., 406, 171. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-12 (mg/ml)
2	1	reservoir	PEG2000	12-17 (%(w/v))
3	1	reservoir	PIPES	0.05-0.08 (M)