6C88

STRUCTURE OF THE AMYLOID FORMING PEPTIDE VAVHVF FROM TRANSTHYRETIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	CCD
Collection date	2014-02-27
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9792
Spacegroup name	P 21 21 21
Unit cell lengths	11.529, 20.360, 36.729
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	18.365 - 1.851
R-factor	0.1723
Rwork	0.171
R-free	0.17850
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	0.827
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (1.12_2829)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	100.000	100.000	1.920
High resolution limit [Å]	1.850	3.990	1.850
Rmerge	0.280	0.089	0.421
Total number of observations	2837
Number of reflections	744	95	71
<I/σ(I)>	3.1
Completeness [%]	84.3	89.6	78.9
Redundancy	3.8	3.5	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	10mg/ml peptide solution. Reservoir contained 0.2 M Magnesium chloride hexahydrate, 0.1 M HEPES sodium pH 7.5, 30% v/v 2-Propanol. Crystals were soaked in 25% glycerol prior to diffraction