SASDVL8 – Glycosidase/Rutinosidase from Mucor circinelloides - deglycosylated monomer

glucan 1,3-beta-glucosidase

MW^experimental	33	kDa
MW^expected	45	kDa
V^Porod	53	nm³

log I(s) 1.16×10^-2 1.16×10^-3 1.16×10^-4 1.16×10^-5

glucan 1,3-beta-glucosidase small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

glucan 1,3-beta-glucosidase Guinier plot

ln 1.17×10^-2 R_g: 2.3 nm 0 (2.3 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 2.3 nm 0 D_max: 6.4 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.3

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.740
1.080

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

glucan 1,3-beta-glucosidase ALPHAFOLD model

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

glucan 1,3-beta-glucosidase DAMMIN model

SAXS data from solutions of Glycosidase/Rutinosidase (deglycosylated monomer) in 50 mM Tris, 150 mM NaCl, pH 7.1 were collected using an Anton Paar SAXSpoint 2.0 instrument at the Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure (Vestec, Czech Republic) equipped with an Eiger R 1M detector at a sample-detector distance of 0.8 m and at a wavelength of λ = 0.134 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). at 20°C. 45 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.

Glycosidase/Rutinosidase from Mucor circinelloides was treated using endo H glycosidase. After SEC, the selected fraction was further concentraced. The raw data are available at: https://doi.org/10.5281/zenodo.13945091

glucan 1,3-beta-glucosidase (McGlcH)
Mol. type		Protein
Organism		Mucor circinelloides
Olig. state		Monomer
Mon. MW		44.7 kDa

UniProt		A0A7M3TUH9 (41-416)
Sequence		FASTA