Standard proteins

Darja Ruskule.

SASDAH2 – Myoglobin in PBS

Myoglobin
MWI(0) 11 kDa
MWexpected 17 kDa
VPorod 32 nm3
log I(s) 1.07×101 1.07×100 1.07×10-1 1.07×10-2
Myoglobin small angle scattering data  s, nm-1
ln I(s)
Myoglobin Guinier plot ln 1.07×101 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
Myoglobin Kratky plot 1.104 0 3 sRg
p(r)
Myoglobin pair distance distribution function Rg: 1.7 nm 0 Dmax: 5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Myoglobin CRYSOL model

log I(s)
 s, nm-1
Myoglobin DAMMIF model

Synchrotron SAXS data from solutions of Myoglobin in PBS in PBS, pH 7.4 were collected on the EMBL X33 beam line at the DORIS III storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.8 and 25 mg/ml were measured at 10°C. Eight successive 15 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

Tags: X33
Myoglobin
Mol. type   Protein
Organism   Equus caballus
Olig. state   Monomer
Mon. MW   17.1 kDa
 
UniProt   P68082
Sequence   FASTA
 
PDB ID   1WLA