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