The flagellotropic bacteriophage YSD1 targets Salmonella Typhi with a Chi-like protein tail fibre.

Dunstan RA, Pickard D, Dougan S, Goulding D, Cormie C, Hardy J, Li F, Grinter R, Harcourt K, Yu L, Song J, Schreiber F, Choudhary J, Clare S, Coulibaly F, Strugnell RA, Dougan G, Lithgow T, Mol Microbiol (2019) Europe PMC

SASDFA6 – Proteolytic fragment of phage flagella binding tail protein YSD1_29 (amino acids 373-1296)

Flagella binding tail protein
MWexperimental 94 kDa
MWexpected 103 kDa
VPorod 155 nm3
log I(s) 2.70×10-1 2.70×10-2 2.70×10-3 2.70×10-4
Flagella binding tail protein small angle scattering data  s, nm-1
ln I(s)
Flagella binding tail protein Guinier plot ln 2.70×10-1 Rg: 5.6 nm 0 (5.6 nm)-2 s2
(sRg)2I(s)/I(0)
Flagella binding tail protein Kratky plot 1.104 0 √3 sRg
p(r)
Flagella binding tail protein pair distance distribution function Rg: 6.1 nm 0 Dmax: 27.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Flagella binding tail protein DAMMIF model
Synchrotron SAXS data from solutions of Proteolytic fragment of phage flagella binding tail protein YSD1_29 (amino acids 373-1296) in 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH 7.8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.4 m and at a wavelength of λ = 0.10322 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAXS was employed. The SEC parameters were as follows: A 100 μl sample at 10 mg/ml was injected onto a GE Superdex 200 Increase 10/300 column at 23°C. 10 successive 1 second frames were collected through the SEC-elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Flagella binding tail protein (YSD1_29)
Mol. type   Protein
Organism   Salmonella virus Chi
Olig. state   Monomer
Mon. MW   102.6 kDa
 
UniProt   M9NVD3 (373-1296)
Sequence   FASTA