Analysis of self-assembly of S-layer protein slp-B53 from Lysinibacillus sphaericus.

Liu J, Falke S, Drobot B, Oberthuer D, Kikhney A, Guenther T, Fahmy K, Svergun D, Betzel C, Raff J, Eur Biophys J 46(1):77-89 (2017) Europe PMC

SASDA69 – slp-B53 with Mg2+

S-layer protein
MWexperimental 178 kDa
MWexpected 116 kDa
VPorod 597 nm3
log I(s) 8.07×103 8.07×102 8.07×101 8.07×100
S-layer protein small angle scattering data  s, nm-1
ln I(s)
S-layer protein Guinier plot ln 8.08×103 Rg: 6.6 nm 0 (6.6 nm)-2 s2
(sRg)2I(s)/I(0)
S-layer protein Kratky plot 1.104 0 √3 sRg
p(r)
S-layer protein pair distance distribution function Rg: 7.3 nm 0 Dmax: 29 nm

Data validation

Fits and models

log I(s)
 s, nm-1
S-layer protein DAMMIF model
log I(s)
 s, nm-1
S-layer protein SASREF MX model
S-layer protein SASREF MX model
Synchrotron SAXS data from solutions of slp-B53 with Mg2+ in Water with Mg2+ were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 7.5 mg/ml were measured at 10°C. 20 successive 0.050 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

Slp-B53 with Mg

S-layer protein (Slp1)
Mol. type   Protein
Organism   Lysinibacillus sphaericus
Olig. state   Monomer
Mon. MW   116.0 kDa
 
UniProt   M4N8T6
Sequence   FASTA