1BZE

TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	296
Detector technology	IMAGE PLATE
Collection date	1996-07-15
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 2
Unit cell lengths	43.470, 86.230, 65.340
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 1.800
R-factor	0.203
Rwork	0.203
R-free	0.27300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tsh
RMSD bond length	0.010
RMSD bond angle	25.500 *
Data reduction software	bioteX
Data scaling software	bioteX
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	52.100	2.000
High resolution limit [Å]	1.800 *	1.700
Rmerge	0.086 *	0.210
Total number of observations	138506 *
Number of reflections	20548 *
<I/σ(I)>	7.2	1.6
Completeness [%]	82.7 *	49
Redundancy	3.0 *	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	23 *	PURIFIED PROTEIN (10MG/ML IN TRIS BUFFER, PH 7.5) WAS CRYSTALLIZED FROM 2M AMMONIUM SULFATE, 100MM CITRATE BUFFER, PH 5.5 AT ROOM TEMPERATURE.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris	0.1 (M)
2	1	drop	protein	10-20 (mg/ml)
3	1	reservoir	ammonium sulfate	1.5-3 (M)
4	1	reservoir	citrate	100 (mM)