1BZD

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	43.400, 86.120, 65.480
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 1.900
R-factor	0.188
Rwork	0.188
R-free	0.26500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tsh
RMSD bond length	0.011
RMSD bond angle	25.700 *
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]	1.700	1.700
Rmerge	0.075	0.210
Total number of observations	146964 *
Number of reflections	19822
<I/σ(I)>	7.2	1.6
Completeness [%]	67.8	49
Redundancy	2.6	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.5	23 *	PURIFIED PROTEIN (20MG/ML IN 25MM MONOBASIC SODIUM PHOSPHATE BUFFER, 0.15M NACL) 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	protein	20 (mg/ml)
2	1	drop	monobasic sodium phosphate	25 (mM)
3	1	drop		0.15 (M)
4	1	reservoir	ammonium sulfate	1.5-3 (M)
5	1	reservoir	citrate	100 (mM)