Extremophilic hemoglobins: The structure of Shewanella benthica truncated hemoglobin N

Martinez Grundman J, Schultz T, Schlessman J, Johnson E, Gillilan R, Lecomte J, Journal of Biological Chemistry :108223 (2025) DOI

SASDWT4 – Shewanella benthica hemoglobin 350 MPa

Group 1 truncated hemoglobin (C51S, C71S)
MWexperimental 12 kDa
MWexpected 13 kDa
VPorod 30 nm3
log I(s) 9.54×10-2 9.54×10-3 9.54×10-4 9.54×10-5
Group 1 truncated hemoglobin (C51S, C71S) small angle scattering data  s, nm-1
ln I(s)
Group 1 truncated hemoglobin (C51S, C71S) Guinier plot ln 9.54×10-2 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
Group 1 truncated hemoglobin (C51S, C71S) Kratky plot 1.104 0 3 sRg
Dmax: 9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Shewanella benthica hemoglobin 350 MPa in 14 mM Tris, 6 mM potassium phosphate, pH 7 were collected on the ID7A1 BioSAXS / HP-Bio Beamline beam line at the Cornell High Energy Synchrotron Source (CHESS) storage ring (Ithaca, NY, USA) using a Eiger 4M detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 0.0883 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 10.00 mg/ml was measured at 23°C. Four 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.

350 MPa hydrostatic pressure.

Group 1 truncated hemoglobin (C51S, C71S) (S2SbHbN)
Mol. type   Protein
Organism   Shewanella benthica KT99
Olig. state   Other
Mon. MW   12.8 kDa
 
UniProt   A9DF82 (2-117)
Sequence   FASTA