Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents.

Kurgan KW, Chen B, Brown KA, Falco Cobra P, Ye X, Ge Y, Gellman SH, Biochemistry 60(14):1108-1119 (2021) Europe PMC

SASDJL9 – Saposin-A monomer

Prosaposin (Saposin A)
MWexperimental 11 kDa
MWexpected 10 kDa
VPorod 23 nm3
log I(s) 1.27×10-2 1.27×10-3 1.27×10-4 1.27×10-5
Prosaposin (Saposin A) small angle scattering data  s, nm-1
ln I(s)
Prosaposin (Saposin A) Guinier plot ln 1.28×10-2 Rg: 1.5 nm 0 (1.5 nm)-2 s2
(sRg)2I(s)/I(0)
Prosaposin (Saposin A) Kratky plot 1.104 0 3 sRg
p(r)
Prosaposin (Saposin A) pair distance distribution function Rg: 1.5 nm 0 Dmax: 5.0 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of monomeric saposin-A in 25 mM Tris-HCl, 150 mM NaCl, pH 7.5 were collected on the 12ID-B SAXS/WAXS beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus 2M detector at a wavelength of λ = 0.0932 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample at 7 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column . 522 successive 1 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.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Prosaposin (Saposin A) (Sap-A)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   9.5 kDa
 
UniProt   P07602 (60-140)
Sequence   FASTA