1III

CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR Y114C-DATA COLLECTED AT ROOM TEMPERATURE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1998-09-03
Detector	MACSCIENCE
Wavelength(s)	1.5418
Spacegroup name	P 21 21 2
Unit cell lengths	43.517, 86.140, 65.554
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.500 * - 2.000
R-factor	0.201
Rwork	0.197
R-free	0.23600 *
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1f41
RMSD bond length	0.008
RMSD bond angle	1.210 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.091	0.398
Total number of observations	155823 *
Number of reflections	17049	1661 *
<I/σ(I)>	8.9	4.3
Completeness [%]	98.5	97.2
Redundancy	5.3	5.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	298	2M ammonium sulphate, 0.1M sodium citrate, 2% PEG 200, 1% BME, pH 5.0, VAPOR DIFFUSION, HANGING DROP at 298K, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3 (mg/ml)
2	1	drop	Tris	50 (mM)	pH7.5
3	1	reservoir	ammonium sulfate	2 (M)
4	1	reservoir	sodium citrate	100 (mM)
5	1	reservoir	PEG200	2 (%)
6	1	reservoir	beta-mercaptoethanol	1 (%)