Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications

Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B, The Journal of Physical Chemistry B (2024) DOI

SASDVC2 – Human Haemoglobin (Sigma-Aldrich) with 5% PEG2000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml

Hemoglobin subunit beta
Hemoglobin subunit alpha
Protoporphyrin IX containing fe
MWexperimental 60295 kDa
MWexpected 32 kDa
VPorod 92 nm3
log I(s) 1.09×10-1 1.09×10-2 1.09×10-3 1.09×10-4
Hemoglobin subunit beta Hemoglobin subunit alpha Protoporphyrin IX containing fe small angle scattering data  s, nm-1
ln I(s)
Hemoglobin subunit beta Hemoglobin subunit alpha Protoporphyrin IX containing fe Guinier plot ln 1.09×10-1 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Hemoglobin subunit beta Hemoglobin subunit alpha Protoporphyrin IX containing fe Kratky plot 1.104 0 3 sRg
p(r)
Hemoglobin subunit beta Hemoglobin subunit alpha Protoporphyrin IX containing fe pair distance distribution function Rg: 2.4 nm 0 Dmax: 6.5 nm

Data validation


There are no models related to this curve.

SAXS data from solutions of Human Haemoglobin (Sigma-Aldrich) with 5% PEG2000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml in 100mM Sodium Phosphate buffer with 5% (w/v) PEG2000, pH 7 were collected using a Eiger R 1M detector at a sample-detector distance of 0.8 m and at a wavelength of λ = 1.34 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 20°C. 30 successive 30 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.

Experimental molecular weight: Size&Shape value from PRIMUS was used.

Hemoglobin subunit beta (human HbB)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   15.9 kDa
 
UniProt   P68871 (2-147)
Sequence   FASTA
 
Hemoglobin subunit alpha (human HbA)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   15.1 kDa
 
UniProt   P69905 (2-142)
Sequence   FASTA
 
Protoporphyrin IX containing fe (Heme B, Haem B)
Mol. type   Other
Olig. state   Monomer
Mon. MW   0.6 kDa
Chemical formula