Thomasclavelia ramosa IgA peptidase (IgAse) active site mutant (A31-I1166)

SASDX42 – IgA peptidase (A31-I1166; active site mutant E540A)

IgA protease (E540A)

MW^experimental	119	kDa
MW^expected	128	kDa
V^Porod	190	nm³

log I(s) 7.01×10¹ 7.01×10⁰ 7.01×10^-1 7.01×10^-2

IgA protease (E540A) small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 7.02×10¹ R_g: 5.7 nm 0 (5.7 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 6.4 nm 0 D_max: 27.9 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.8

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.203
1.053

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

IgA peptidase (A31-I1166; active site mutant E540A) Rg histogram

R_g, nm

Synchrotron SAXS data from solutions of IgA peptidase in 50 mM Tris, 150 mM NaCl, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured at 20°C. 250 successive 4 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 results obtained from EOM analysis are made available in the full entry zip archive.

IgA protease (E540A) (IgAse)
Mol. type		Protein
Organism		Thomasclavelia ramosa
Olig. state		Monomer
Mon. MW		127.9 kDa

UniProt		Q9AES2 (31-1166)
Sequence		FASTA