| MWexperimental | 42 | kDa |
| MWexpected | 42 | kDa |
| VPorod | 58 | nm3 |
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log I(s)
2.69×10-2
2.69×10-3
2.69×10-4
2.69×10-5
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s, nm-1
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Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I, Biochemical and Biophysical Research Communications :149340 (2023) DOISASDTX4 – G-actin - Skeletal muscle actin from Oryctolagus cuniculus: globular actin monomers
Actin, alpha skeletal muscle|
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Fits and models
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SAXS data from solutions of G-actin from Oryctolagus cuniculus (globular actin monomers) in 5 mM Tris/Tris-HCl, 0.1 mM CaCl2, 1 mM NaN3, 0.2 mM ATP, pH 8.1 were collected using a Rigaku MicroMax 007-HF instrument at the Moscow Institute of Physics and Technology (MIPT; Dolgoprudny, Russian Federation) equipped with a multiwire gas-filled ASM DTR Triton 200 detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.15406 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.3 and 1.3 mg/ml were measured at 20°C. One 3600 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Approximation of SAXS data at 1.25 mg/ml using G-actin atomic model (PDB ID: 3HBT) with CRYSOL program featured good quality of fit, which indicates that the starting material is G-actin. |
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