6GR7

Crystal Structure Of Human Transthyretin in complex with 2,4,5-trichlorophenoxyacetic acid (2,4,5-T)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-3
Synchrotron site	ESRF
Beamline	MASSIF-3
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-03-09
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.968
Spacegroup name	P 21 21 2
Unit cell lengths	42.878, 85.486, 64.488
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.700 - 1.400
R-factor	0.1696
Rwork	0.169
R-free	0.18770
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f41
RMSD bond length	0.009
RMSD bond angle	0.914
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.700	1.450
High resolution limit [Å]	1.400	1.400
Rmerge	0.073	1.070
Number of reflections	46647	4301
<I/σ(I)>	17.3	2.2
Completeness [%]	98.5	89.9
Redundancy	13.3	10.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.5	291	The purified human TTR was dialyzed against 10 mM Na-phosphate buffer with 100 mM KCl (pH 7.6) and concentrated to 5 mg/mL The reservoir contained 28% PEG 4K, 0.1M NaAc pH 4.5, 0.2M AmAc. Drop size 3 plus 3 microliter.