Self-assembly and regulation of protein cages from pre-organised coiled-coil modules.

Lapenta F, Aupič J, Vezzoli M, Strmšek Ž, Da Vela S, Svergun DI, Carazo JM, Melero R, Jerala R, Nat Commun 12(1):939 (2021) Europe PMC

SASDJV5 – SBP12(9.b)

SBP1(9.b)
SBP2(9.b)
MWexperimental 83 kDa
MWexpected 80 kDa
log I(s) 3.45×101 3.45×100 3.45×10-1 3.45×10-2
SBP1(9.b) SBP2(9.b) small angle scattering data  s, nm-1
ln I(s)
SBP1(9.b) SBP2(9.b) Guinier plot ln 3.45×101 Rg: 4 nm 0 (4 nm)-2 s2
(sRg)2I(s)/I(0)
SBP1(9.b) SBP2(9.b) Kratky plot 1.104 0 3 sRg
p(r)
SBP1(9.b) SBP2(9.b) pair distance distribution function Rg: 3.9 nm 0 Dmax: 11.8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
SBP1(9.b) SBP2(9.b) MODELLER model

log I(s)
 s, nm-1
SBP1(9.b) SBP2(9.b) DAMMIN model

Synchrotron SAXS data from solutions of SBP12(9.b) in 20 mM Tris 150 mM NaCl 10% glycerol, pH 7.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS, Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A sample at 9.2 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 10/300 column at 25°C. 1000 successive 3 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.

SBP1(9.b)
Mol. type   Protein
Organism   synthetic construct
Olig. state   Monomer
Mon. MW   40.0 kDa
Sequence   FASTA
 
SBP2(9.b)
Mol. type   Protein
Organism   synthetic construct
Olig. state   Monomer
Mon. MW   40.4 kDa
Sequence   FASTA