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

SASDF38 – Myotilin immunoglobulin domains Ig1Ig2 (250-444)

Myotilin Ig1Ig2 (250-444)
MWI(0) 17 kDa
MWexpected 22 kDa
VPorod 29 nm3
log I(s) 1.73×101 1.73×100 1.73×10-1 1.73×10-2
Myotilin Ig1Ig2 (250-444) small angle scattering data  s, nm-1
ln I(s)
Myotilin Ig1Ig2 (250-444) Guinier plot ln 1.73×101 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
Myotilin Ig1Ig2 (250-444) Kratky plot 1.104 0 3 sRg
p(r)
Myotilin Ig1Ig2 (250-444) pair distance distribution function Rg: 2.9 nm 0 Dmax: 10.1 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Myotilin Ig1Ig2 (250-444) 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 14.12 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Myotilin Ig1Ig2 (250-444) (Ig1Ig2 (250-444))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   22.3 kDa
 
UniProt   Q9UBF9 (250-444)
Sequence   FASTA