Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo.

Ljubetič A, Lapenta F, Gradišar H, Drobnak I, Aupič J, Strmšek Ž, Lainšček D, Hafner-Bratkovič I, Majerle A, Krivec N, Benčina M, Pisanski T, Veličković TĆ, Round A, Carazo JM, Melero R, Jerala R, Nat Biotechnol 35(11):1094-1101 (2017) Europe PMC

SASDBS9 – TET12SN

TET12(1.10)SN-f5

MW^I(0)	51	kDa
MW^expected	53	kDa
V^Porod	107	nm³

log I(s) 5.11×10¹ 5.11×10⁰ 5.11×10^-1 5.11×10^-2

TET12(1.10)SN-f5 small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 5.11×10¹ R_g: 3.5 nm 0 (3.5 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 3.5 nm 0 D_max: 12 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.4

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0
0.607

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Synchrotron SAXS data from solutions of TET12SN in 20 mM Tris, 150 mM NaCl, 10% glycerol, pH 7.5, were collected at the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.89 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, where 2θ is the scattering angle). A solute concentration series ranging between 0.9 and 3.6 mg/ml were measured at 20°C. For each sample, data was collected over 10 frames lasting 1 or 2 s. The data were normalized to the intensity of the transmitted beam and radially averaged. Each individual frames were carefully inspected for radiation damage and those not showing any radiation damage were then averaged. The scattering of the matched solvent-blank was subtracted and the different curves were scaled for protein concentration. Scattering curves were merged and analyzed using PRIMUS software.

TET12(1.10)SN-f5 (TET12SN)
Mol. type		Protein
Organism		synthetic construct
Olig. state		Monomer
Mon. MW		53.4 kDa
Sequence		FASTA