Microtubule plus-end regulation by centriolar cap proteins

Ogunmolu F, Moradi S, Volkov V, van Hoorn C, Wu J, Andrea N, Hua S, Jiang K, Vakonakis I, Potocnjak M, Herzog F, Gigant B, Gudimchuk N, Stecker K, Dogterom M, Steinmetz M, Akhmanova A, (2021) DOI

SASDNB3 – Homodimerisation of the CP110 C-terminus coiled-coil domain

Centriolar coiled-coil protein of 110 kDa
MWexperimental 18 kDa
MWexpected 20 kDa
VPorod 33 nm3
log I(s) 3.11×10-2 3.11×10-3 3.11×10-4 3.11×10-5
Centriolar coiled-coil protein of 110 kDa small angle scattering data  s, nm-1
ln I(s)
Centriolar coiled-coil protein of 110 kDa Guinier plot ln 3.12×10-2 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Centriolar coiled-coil protein of 110 kDa Kratky plot 1.104 0 √3 sRg
p(r)
Centriolar coiled-coil protein of 110 kDa pair distance distribution function Rg: 3.6 nm 0 Dmax: 12.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Centriolar coiled-coil protein of 110 kDa DAMMIF model
Synchrotron SAXS data from solutions of the CP110 C-terminus coiled-coil domain in 50 mM HEPES, pH 7.5, 100 mM NaCl, 1 mM DTT, 1 mM MgCl2, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 80.00 μl sample at 10 mg/ml was injected onto a Shodex KW402.5-4F column at 25°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. SEC flow rate = UNKNOWN.

Centriolar coiled-coil protein of 110 kDa (CP110)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   10.0 kDa
 
UniProt   O43303 (635-717)
Sequence   FASTA