1TSH

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

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	296
Detector technology	IMAGE PLATE
Collection date	1994-07
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 2
Unit cell lengths	43.890, 86.170, 65.460
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	5.000 - 1.700
R-factor	0.189
Rwork	0.189
R-free	0.24800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tta
RMSD bond length	0.009
RMSD bond angle	1.740
Data reduction software	bioteX
Data scaling software	bioteX
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	52.130	2.000
High resolution limit [Å]	1.700	1.700
Rmerge	0.085	0.240
Number of reflections	24555
<I/σ(I)>	10	2.4
Completeness [%]	87.4	77
Redundancy	2.9	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		5.5		PURIFIED PROTEIN (20MG/ML IN 25MM MONOBASIC SODIUM PHOSPHATE BUFFER, 0.15M NACL) WAS CRYSTALLIZED FROM 2.5M AMMONIUM SULFATE, 100MM CITRATE BUFFER, PH 5.5 AT ROOM TEMPERATURE.