5AL0

Transthyretin binding heterogeneity and anti-amyloidogenic activity of natural polyphenols and their metabolites: resveratrol-3-O-sulfate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	PIXEL
Detector	DECTRIS PAD P2M
Spacegroup name	P 21 21 2
Unit cell lengths	42.814, 85.569, 64.122
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.785 - 1.388
R-factor	0.173
Rwork	0.171
R-free	0.20890
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f41
RMSD bond length	0.008
RMSD bond angle	1.180
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.780	1.460
High resolution limit [Å]	1.390	1.390
Rmerge	0.030	0.370
Number of reflections	45697
<I/σ(I)>	22.8	3.2
Completeness [%]	96.8	93.4
Redundancy	3.4	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7		CRYSTALS OF WT HUMAN TTR- LIGAND COMPLEXES WERE OBTAINED AT ROOM TEMPERATURE IN ABOUT ONE WEEK BY CO-CRYSTALLIZATION, USING THE HANGING-DROP VAPOR DIFFUSION METHOD. THE PROTEIN (5 MG/ML), IN 20 MM SODIUM PHOSPHATE, PH 7, WAS INCUBATED WITH A FOUR-FOLD MOLAR EXCESS OF LIGANDS SOLUBILIZED IN DMSO. DROPS WERE FORMED BY MIXING EQUAL VOLUMES OF THE SOLUTION CONTAINING LIGAND-TTR COMPLEXES AND OF THE RESERVOIR/PRECIPITANT SOLUTION (2.2 M AMMONIUM SULPHATE, 0.1 M KCL, 0.03 M SODIUM PHOSPHATE, PH 7.0).