3TCY

Crystallographic structure of phenylalanine hydroxylase from Chromobacterium violaceum (cPAH) bound to 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	2011-03-27
Detector	MAR scanner 300 mm plate
Wavelength(s)	1.033
Spacegroup name	P 1
Unit cell lengths	36.674, 38.281, 47.736
Unit cell angles	76.65, 73.03, 85.69

Refinement procedure

Resolution	37.250 - 1.550
R-factor	0.16488
Rwork	0.163
R-free	0.20698
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ltu
RMSD bond length	0.011
RMSD bond angle	1.400
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	1.580
High resolution limit [Å]	1.550	1.550
Rmerge	0.036
Number of reflections	31363
<I/σ(I)>	26.2
Completeness [%]	95.0	84.6
Redundancy	2.3

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