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

SASDWM4 – Shewanella benthica hemoglobin 0.101 MPa (final measurement after end of pressure series)

Group 1 truncated hemoglobin (C51S, C71S)
MWexperimental 30 kDa
MWexpected 13 kDa
VPorod 70 nm3
log I(s) 2.87×10-1 2.87×10-2 2.87×10-3 2.87×10-4
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 2.88×10-1 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: 7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Shewanella benthica hemoglobin 0.101 MPa (final measurement after end of pressure series) 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.

Final measurement returned to 0.101 MPa (1 standard atmosphere) after pressure series.

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