2TRH

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	1995-06
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 2
Unit cell lengths	43.380, 86.340, 65.580
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	5.000 - 1.900
R-factor	0.219
Rwork	0.219
R-free	0.29900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tta
RMSD bond length	0.011
RMSD bond angle	1.870
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]	52.220	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.109	0.270
Number of reflections	20855
<I/σ(I)>	5	1.9
Completeness [%]	88.6	74.7
Redundancy	4.3	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		6.5		PURIFIED PROTEIN (20MG/ML IN 100MM TRIS BUFFER, PH 7.5) WAS CRYSTALLIZED FROM\\ 2.25M AMMONIUM SULFATE, 100MM CITRATE BUFFER, PH 5.5 AT ROOM TEMPERATURE.\\, pH 6.5