Rabbit muscle fructose-1,6-bisphosphate aldolase K229M mutant

Normand Cyr.

SASDFR7 – Rabbit muscle fructose-bisphosphate aldolase A, K229M mutant

Fructose-bisphosphate aldolase A
MWI(0) 160 kDa
MWexpected 157 kDa
VPorod 213 nm3
log I(s) 1.30×10-1 1.30×10-2 1.30×10-3 1.30×10-4
Fructose-bisphosphate aldolase A small angle scattering data  s, nm-1
ln I(s)
Fructose-bisphosphate aldolase A Guinier plot ln 1.30×10-1 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Fructose-bisphosphate aldolase A Kratky plot 1.104 0 √3 sRg
p(r)
Fructose-bisphosphate aldolase A pair distance distribution function Rg: 3.6 nm 0 Dmax: 11.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Fructose-bisphosphate aldolase A PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
Fructose-bisphosphate aldolase A DAMMIN model
SAXS data from solutions of rabbit muscle fructose-bisphosphate aldolase A (K229M) in 20 mM HEPES, pH 7 were collected using Xenocs BioXolver L instrument with MetalJet (Département de Biochimie, Université de Montréal, Canada) with a Pilatus3 R 300K detector at a wavelength of λ = 1.348 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.66 mg/ml was measured at 20°C. 10 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.

Fructose-bisphosphate aldolase A (Aldolase)
Mol. type   Protein
Organism   Oryctolagus cuniculus
Olig. state   Tetramer
Mon. MW   39.2 kDa
 
UniProt   P00883 (2-364)
Sequence   FASTA
 
PDB ID   5F4X