Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic

Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R, Biophysical Journal 94(1):173-181 (2008) DOI

SASDNT2 – Experimental SAXS data for native hemoglobin (Hb) at concentration c = 31.25 mg/ml

Hemoglobin subunit alpha
Hemoglobin subunit beta
MWexperimental 47 kDa
MWexpected 31 kDa
log I(s) 1.09×101 1.09×100 1.09×10-1 1.09×10-2
Hemoglobin subunit alpha Hemoglobin subunit beta small angle scattering data  s, nm-1
ln I(s)
Hemoglobin subunit alpha Hemoglobin subunit beta Guinier plot ln 1.10×101 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
Hemoglobin subunit alpha Hemoglobin subunit beta Kratky plot 1.104 0 3 sRg

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Experimental SAXS data for native hemoglobin (Hb) at concentration c = 31.25 mg/ml in Ringer's lactate solution, pH 6.5 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 31.25 mg/ml was measured. Three successive 60 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.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Tags: X33
Hemoglobin subunit alpha (Hba)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   15.0 kDa
 
UniProt   P69905 (3-142)
Sequence   FASTA
 
Hemoglobin subunit beta (Hbb)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   15.8 kDa
 
UniProt   P68871 (3-147)
Sequence   FASTA