Molecular basis of F-actin regulation and sarcomere assembly via myotilin

Kostan J, Pavšič M, Puž V, Schwarz T, Drepper F, Molt S, Graewert M Schreiner C, Sajko S, van der Ven P, Onipe A, Svergun D, Warscheid B, Konrat R, Fürst D, Lenarčič B, Djinović-Carugo K, Machesky L, PLOS Biology 19(4):e3001148 (2021) DOI

SASDF28 – Myotilin immunoglobulin domains Ig1Ig2 (220-452)

Myotilin Ig1Ig2 (220-452)
MWexperimental 26 kDa
MWexpected 27 kDa
VPorod 52 nm3
log I(s) 2.63×101 2.63×100 2.63×10-1 2.63×10-2
Myotilin Ig1Ig2 (220-452) small angle scattering data  s, nm-1
ln I(s)
Myotilin Ig1Ig2 (220-452) Guinier plot ln 2.63×101 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Myotilin Ig1Ig2 (220-452) Kratky plot 1.104 0 3 sRg
p(r)
Myotilin Ig1Ig2 (220-452) pair distance distribution function Rg: 3.9 nm 0 Dmax: 15.1 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of myotilin Ig1Ig2 (220-452) in 20 mM Na+-HEPES, 150 mM, NaCl, 5 % v/v glycerol, 1 mM DTT, pH 7.4 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 21.00 mg/ml was measured at 20°C. 15 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.

Storage temperature = UNKNOWN

Myotilin Ig1Ig2 (220-452) (Ig1Ig2 (220-452))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   26.5 kDa
 
UniProt   Q9UBF9 (220-452)
Sequence   FASTA