7THA

Crystal structure of human transthyretin variant C10A/M13V

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2017-05-22
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.5418
Spacegroup name	P 21 2 21
Unit cell lengths	42.602, 64.509, 85.919
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.870 - 1.750
R-factor	0.1829
Rwork	0.181
R-free	0.21110
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ydm
RMSD bond length	0.011
RMSD bond angle	1.670
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.8.0238)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.960	1.840
High resolution limit [Å]	1.750	1.750
Rpim	0.026	0.590
Number of reflections	24607	3541
<I/σ(I)>	17.3	1.6
Completeness [%]	100.0
Redundancy	7.7
CC(1/2)	1.000	0.730

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		298	Crystals of TTR C10A/M13V were grown at 23 degrees C using sitting-drop vapor diffusion by mixing 0.2 microliters of 5 mg/mL protein in 50 mM Tris pH 7.8 and 0.2 microliters of a crystallization buffer consisting of 0.19M CaCl2, 5% (v/v) glycerol, 0.095M HEPES pH 7.5, and 26.6% (v/v) PEG 400. Crystals were frozen directly without additional cryo-protection by plunging in liquid nitrogen