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