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

SASDJQ9 – Saposin-B, R232W mutant

Prosaposin (Saposin-B, R232W mutant)
MWexperimental 20 kDa
MWexpected 18 kDa
log I(s) 2.30×10-2 2.30×10-3 2.30×10-4 2.30×10-5
Prosaposin (Saposin-B, R232W mutant) small angle scattering data  s, nm-1
ln I(s)
Prosaposin (Saposin-B, R232W mutant) Guinier plot ln 2.31×10-2 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Prosaposin (Saposin-B, R232W mutant) Kratky plot 1.104 0 3 sRg
p(r)
Prosaposin (Saposin-B, R232W mutant) pair distance distribution function Rg: 1.9 nm 0 Dmax: 5.8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of saposin-B, R232W mutant 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 10 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column . 801 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-B, R232W mutant) (Sap-B, R232W)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   9.2 kDa
 
UniProt   P07602 (195-272)
Sequence   FASTA