Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes.

Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish, Int J Biol Macromol :134556 (2024) Europe PMC

SASDU24 – Calcium activated full-length gelsolin and the F-form of actin at a 1:8 molar ratio in F-actin buffer

Gelsolin
Actin, cytoplasmic 1
MWexperimental 585 kDa
MWexpected 836 kDa
log I(s) 5.83×104 5.83×103 5.83×102 5.83×101
Gelsolin Actin, cytoplasmic 1 small angle scattering data  s, nm-1
ln I(s)
Gelsolin Actin, cytoplasmic 1 Guinier plot ln 5.83×104 Rg: 13.6 nm 0 (13.6 nm)-2 s2
(sRg)2I(s)/I(0)
Gelsolin Actin, cytoplasmic 1 Kratky plot 1.104 0 √3 sRg

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Calcium activated full-length gelsolin and the F-form of actin at a 1:8 molar ratio in F-actin buffer in 50 mM KCl, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2, 1 mM ATP, 0.1% 2-mercaptoethanol, pH 8 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.155 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 10°C. 20 successive 0.050 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.

Gelsolin (rhuGSN)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   84.3 kDa
 
UniProt   P06396 (25-782)
Sequence   FASTA
 
Actin, cytoplasmic 1
Mol. type   Protein
Organism   Gallus gallus
Olig. state   18-mer
Mon. MW   41.7 kDa
 
UniProt   P60706 (1-375)
Sequence   FASTA