5L4I

Crystal Structure of Human Transthyretin in Complex with Clonixin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-05-02
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.873
Spacegroup name	P 21 21 2
Unit cell lengths	43.083, 86.275, 64.297
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.544 - 1.450
R-factor	0.1436
Rwork	0.142
R-free	0.17860
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f41
RMSD bond length	0.008
RMSD bond angle	0.900
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]	43.100	1.470
High resolution limit [Å]	1.450	1.450
Rmerge	0.068	1.135
Number of reflections	43302
<I/σ(I)>	12.8	1.4
Completeness [%]	100.0	100
Redundancy	6.2	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.6	291	Purified TTRwt was dialyzed against 10 mM sodiumphosphate buffer with 100 mM KCl pH 7.6 and concentrated to 5 mg per ml. Clonixin was added at 5 x molar excess to the protein. The reservoir contained 1.3 to 1.6 M sodium citrate and 3.5 percent glycerol at pH 5.5. Drop size 3 plus 3 microliter