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

SASDCZ7 – TET12(1.6)S-c6b

TET12(1.6)S-c6b
MWI(0) 53 kDa
MWexpected 54 kDa
VPorod 114 nm3
log I(s) 7.25×103 7.25×102 7.25×101 7.25×100
TET12(1.6)S-c6b small angle scattering data  s, nm-1
ln I(s)
TET12(1.6)S-c6b Guinier plot ln 7.26×103 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
TET12(1.6)S-c6b Kratky plot 1.104 0 √3 sRg
p(r)
TET12(1.6)S-c6b pair distance distribution function Rg: 3.6 nm 0 Dmax: 11.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
TET12(1.6)S-c6b MODELLER model
Synchrotron SAXS data from solutions of TET12(1.6)S-c6b in 20 mM Tris 150 mM NaCl 10% glycerol, pH 7.5 were collected on the P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 1M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). Solute concentrations ranging between 1 and 5 mg/ml were measured at 20°C. 20 successive 0.045 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration. Scattering curves were merged and analyzed using PRIMUS software.

Concentration min = UNKNOWN

TET12(1.6)S-c6b
Mol. type   Protein
Organism   synthetic construct
Olig. state   Monomer
Mon. MW   54.5 kDa
Sequence   FASTA