K -edge anomalous SAXS for protein solution structure modeling

Virk K, Yonezawa K, Choukate K, Singh L, Shimizu N, Chaudhuri B, Acta Crystallographica Section D Structural Biology 78(2) (2022) DOI

SASDMC8 – Poly-histidine tagged Myosin X component with CuSO4 at 8987 eV

Unconventional myosin-X component
MWexperimental 18 kDa
MWexpected 15 kDa
VPorod 28 nm3
log I(s) 1.14×10-1 1.14×10-2 1.14×10-3 1.14×10-4
Unconventional myosin-X component small angle scattering data  s, nm-1
ln I(s)
Unconventional myosin-X component Guinier plot ln 1.15×10-1 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Unconventional myosin-X component Kratky plot 1.104 0 3 sRg
Dmax: 11 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Poly-histidine tagged Myosin X component with CuSO4 at 8987 eV in HEPES, 5% glycerol, 150 mM NaCl, pH 7.4 were collected on the BL-15A2 beam line at the Photon Factory (PF), High Energy Accelerator Research Organization (KEK) storage ring (Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 1.6 m and at a wavelength of λ = 0.137959 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.87 mg/ml was measured at 20°C. 180 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.

Poly-histidine tagged Myosin X component with CuSO4 at 8987 eV, not corrected for X-ray fluorescence. The data were put to absolute scale with water scattering data collected at the same X-ray energy.

Unconventional myosin-X component (Myo10antiCC)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   7.7 kDa
 
UniProt   Q9HD67 (883-933)
Sequence   FASTA