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

SASDCT7 – PYR16(4.6)SN-f5

PYR16(4.6)SN-f5
MWI(0) 65 kDa
MWexpected 72 kDa
VPorod 136 nm3
log I(s) 6.53×101 6.53×100 6.53×10-1 6.53×10-2
PYR16(4.6)SN-f5 small angle scattering data  s, nm-1
ln I(s)
PYR16(4.6)SN-f5 Guinier plot ln 6.54×101 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
PYR16(4.6)SN-f5 Kratky plot 1.104 0 √3 sRg
p(r)
PYR16(4.6)SN-f5 pair distance distribution function Rg: 3.8 nm 0 Dmax: 11.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
PYR16(4.6)SN-f5 MODELLER model
Synchrotron SAXS data from solutions of PYR16SN 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 1 and 7.6 mg/ml were measured at 20°C. For each sample, data was collected over 10 frames lasting 1 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 analyzed using PRIMUS software.

PYR16(4.6)SN-f5
Mol. type   Protein
Organism   synthetic construct
Olig. state   Monomer
Mon. MW   71.7 kDa
Sequence   FASTA