6C3T

AMYLOID FORMING PEPTIDE AADTWE FROM TRANSTHYRETIN WITH ATTR-D38A MUTATION ASSOCIATED WITH A FAMILIAL FORM OF TRANSTHYRETIN AMYLOIDOSIS

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	2008-10-29
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9792
Spacegroup name	P 1 21 1
Unit cell lengths	9.019, 43.157, 9.392
Unit cell angles	90.00, 102.84, 90.00

Refinement procedure

Resolution	21.580 - 1.000
R-factor	0.1107
Rwork	0.109
R-free	0.12400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Ideal beta strand
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.4.0061)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	90.000	90.000	1.080
High resolution limit [Å]	1.000	1.710	1.000
Rmerge	0.128	0.089	0.397
Number of reflections	3204	766	353
<I/σ(I)>	11.7
Completeness [%]	83.5	96.7	46.8
Redundancy	13.9	14.1	10.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	AADTWE crystals were grown from a solution containing 100 mg/ml peptide. The reservoir contained 0.2 M Ammonium phosphate monobasic, 0.1 M Tris pH 8.5, and 50 % v/v MPD. Crystals were soaked on 25% Glycerol prior to diffraction