Structural flexibility of the tetanus neurotoxin revealed by crystallographic and solution scattering analyses.

Zhang CM, Imoto Y, Hikima T, Inoue T, J Struct Biol X 5:100045 (2021) Europe PMC

SASDJP5 – Beltless isolated translocation domain of tetanus nerotoxin (TeNT/blHn)

Tetanus toxin
MWexperimental 33 kDa
MWexpected 35 kDa
VPorod 42 nm3
log I(s) 1.39×10-2 1.39×10-3 1.39×10-4 1.39×10-5
Tetanus toxin small angle scattering data  s, nm-1
ln I(s)
Tetanus toxin Guinier plot ln 1.40×10-2 Rg: 2.9 nm 0 (2.9 nm)-2 s2
Tetanus toxin Kratky plot 1.104 0 3 sRg
Tetanus toxin pair distance distribution function Rg: 3.1 nm 0 Dmax: 11.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Tetanus toxin PDB (PROTEIN DATA BANK) model

log I(s)
 s, nm-1
Tetanus toxin DAMMIN model

Synchrotron SAXS data from solutions of the beltless isolated translocation domain of the tetanus nerotoxin (TeNT/blHn) in 10 mM HEPES 100 mM NaCl, pH 7.4 were collected on the BL45XU beam line at SPring-8 (Hyōgo Prefecture, Japan) using a Pilatus3 X 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1 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 100.00 μl sample at 5 mg/ml was injected at a 0.75 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 800 successive 0.500 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.

Storage temperature = UNKNOWN

Tetanus toxin (TeNT/blHn)
Mol. type   Protein
Organism   Clostridium tetani
Olig. state   Monomer
Mon. MW   34.6 kDa
UniProt   P04958 (564-864)
Sequence   FASTA