On the Occurrence and Multimerization of Two-Polypeptide Phage Endolysins Encoded in Single Genes.

Pinto D, Gonçalo R, Louro M, Silva MS, Hernandez G, Cordeiro TN, Cordeiro C, São-José C, Microbiol Spectr :e0103722 (2022) Europe PMC

SASDNU5 – Lysin from Streptococcus phage P7951 ∆1-208

lysin [Streptococcus phage P7951]
MWexperimental 70 kDa
MWexpected 65 kDa
VPorod 111 nm3
log I(s) 7.00×101 7.00×100 7.00×10-1 7.00×10-2
lysin [Streptococcus phage P7951] small angle scattering data  s, nm-1
ln I(s)
lysin [Streptococcus phage P7951] Guinier plot ln 7.01×101 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
lysin [Streptococcus phage P7951] Kratky plot 1.104 0 √3 sRg
p(r)
lysin [Streptococcus phage P7951] pair distance distribution function Rg: 3.1 nm 0 Dmax: 10.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
lysin [Streptococcus phage P7951] DAMFILT model
Synchrotron SAXS data from solutions of Lysin from Streptococcus phage P7951 ∆1-208 in 50 mM HEPES, 500 mM NaCl, and 1% glycerol, pH 7 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.70 mg/ml was measured at 20°C. 10 successive 1 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.

Lysin from Streptococcus phage P7951 (amino acids 209-310) with a C-terminal His-tag. The bead model displayed in this entry is the volume and bead occupancy-corrected spatial representation of the protein obtained from the spatial alignment of several individual models and does not reflect the fit to the SAXS data.

lysin [Streptococcus phage P7951] (LysP7951)
Mol. type   Protein
Organism   Streptococcus phage P7951
Olig. state   Hexamer
Mon. MW   10.8 kDa
Sequence   FASTA