1MLW

Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-1
Synchrotron site	SSRL
Beamline	BL9-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-05-05
Detector	MARRESEARCH
Wavelength(s)	0.954
Spacegroup name	P 21 21 21
Unit cell lengths	47.775, 57.334, 109.410
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.710
Rwork	0.205
R-free	0.23100 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pah
RMSD bond length	0.005
RMSD bond angle	1.200
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *	1.770
High resolution limit [Å]	1.710	1.710
Rmerge	0.099	0.010
Total number of observations	320396 *
Number of reflections	32923	3215 *
<I/σ(I)>	32	2.5
Completeness [%]	99.2	98.4
Redundancy	9	9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	4 *	16-18% MPEG5000, 25-40 mM MES buffer, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	mPEG5000	16-18 (%)
2	1	reservoir	MES	25-40 (mM)	pH6.0