5K1N

Human TTR altered by a rhenium tris-carbonyl Pyta-C12 derivative

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 2
Synchrotron site	SOLEIL
Beamline	PROXIMA 2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-04-22
Detector	DECTRIS EIGER X 9M
Wavelength(s)	1.175919
Spacegroup name	P 21 21 2
Unit cell lengths	42.650, 82.130, 67.720
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.065 - 1.810
R-factor	0.1906
Rwork	0.189
R-free	0.22390
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5k1j
RMSD bond length	0.005
RMSD bond angle	0.819
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	REFMAC
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.860
High resolution limit [Å]	1.810	1.810
Rmerge	0.065	0.782
Number of reflections	41147
<I/σ(I)>	12.31	1.69
Completeness [%]	98.2	98.4
Redundancy	2.6	2.6
CC(1/2)	0.998

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	293	protein: 10 mg/ml Dialysed in 100 milli-M NaCl, 50 milli-M sodium acetate, pH 5.5 precipitant: 21% polyethylene glycol 4,000 (PEG4K), 0.14 M imidazole malate, pH 6.0 + 3.6% polyethylene glycol monomethyl ether (MPEG5K), 30 mM sodium acetate pH 5.5 cryosoak: 40% SM3 (25 % diethylene glycol + 25 % ethylene glycol + 25 % glycerol + 25 % 1,4-dioxane) 50% PEG 8K and 0.5 milli-M of rhenium tris-carbonyl Pyta-C12 derivative.