Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A.

Zeng B, Mou TC, Doukov TI, Steiner A, Yu W, Papasergi-Scott M, Tall GG, Hagn F, Sprang SR, Structure (2019) Europe PMC

SASDFA5 – Unposphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)

Resistance to inhibitors of cholinesterase 8 homolog A
MWexperimental 51 kDa
MWexpected 51 kDa
VPorod 70 nm3
log I(s) 8.45×101 8.45×100 8.45×10-1 8.45×10-2
Resistance to inhibitors of cholinesterase 8 homolog A small angle scattering data  s, nm-1
ln I(s)
Resistance to inhibitors of cholinesterase 8 homolog A Guinier plot ln 8.46×101 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Resistance to inhibitors of cholinesterase 8 homolog A Kratky plot 1.104 0 3 sRg
p(r)
Resistance to inhibitors of cholinesterase 8 homolog A pair distance distribution function Rg: 3.0 nm 0 Dmax: 10.6 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of unposphorylated Ric-8A (amino acids 1-452) in 25mM HEPES, 150mM NaCl, pH 8 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (SSRL; Stanford, CA, USA) using a Rayonix MX225-HE detector at a sample-detector distance of 1.7 m and at a wavelength of λ = 0.1127 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 25 °C using the following parameters: Column: Superdex 200 Increase 3.2/300 analytical SEC column; Flow rate: 0.05 mL/min; Sample injection concentration: 1.0 mg/mL; Injection volume: 100 μL. The data were collected through the SEC peak of the sample as a series of 5 x 1 second exposures. Each unsubtracted data frame was normalised to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile displayed in this entry.

CAUTION! The data used to calculate p(r) profile are different to primary SAXS data.

Resistance to inhibitors of cholinesterase 8 homolog A (Ric-8A)
Mol. type   Protein
Organism   Rattus norvegicus
Olig. state   Monomer
Mon. MW   51.1 kDa
 
UniProt   B1H241 (1-452)
Sequence   FASTA