3TK2

Crystallographic structure of phenylalanine hydroxylase from Chromobacterium violaceum cocrystallized with phenylalanine in a site distal to the active site

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2011-06-26
Detector	MAR scanner 300 mm plate
Wavelength(s)	1.033
Spacegroup name	P 1
Unit cell lengths	36.934, 38.561, 47.800
Unit cell angles	76.56, 72.90, 85.41

Refinement procedure

Resolution	24.490 - 1.350
R-factor	0.16098
Rwork	0.159
R-free	0.20727
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ltu
RMSD bond length	0.025
RMSD bond angle	2.199
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MOLREP
Refinement software	REFMAC (5.5.0110)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.370
High resolution limit [Å]	1.350	1.350
Rmerge	0.043
Number of reflections	47843
<I/σ(I)>	34.2
Completeness [%]	93.5	84
Redundancy	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	0.1M Na-HEPES, 0.001M Magnesium chloride hexahydrate, 0.005M Nickel (II) chloride hexahydrate, 15% w/v PEG 3,350, 0.1M hexammine cobalt (II) chloride, 1.0M guanidine hydrochloride, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K