Structural basis of microtubule-mediated signal transduction.

Choi SR, Blum TB, Giono M, Roy B, Vakonakis I, Schmid D, Oelgarth N, Ranganathan A, Gossert AD, Shivashankar GV, Zippelius A, Steinmetz MO, Cell (2025) Europe PMC

SASDV33 – N-terminal domain construct of hsGEFH1_190-582aa fit to DAMMIF and Alphafold2 models

Isoform 1 of Rho guanine nucleotide exchange factor 2
MWexperimental 41 kDa
MWexpected 47 kDa
log I(s) 7.09×10-3 7.09×10-4 7.09×10-5 7.09×10-6
Isoform 1 of Rho guanine nucleotide exchange factor 2 small angle scattering data  s, nm-1
ln I(s)
Isoform 1 of Rho guanine nucleotide exchange factor 2 Guinier plot ln 7.09×10-3 Rg: 5.9 nm 0 (5.9 nm)-2 s2
(sRg)2I(s)/I(0)
Isoform 1 of Rho guanine nucleotide exchange factor 2 Kratky plot 1.104 0 3 sRg

Data validation


Fits and models


log I(s)
 s, nm-1
Isoform 1 of Rho guanine nucleotide exchange factor 2 ALPHAFOLD model

log I(s)
 s, nm-1
Isoform 1 of Rho guanine nucleotide exchange factor 2 DAMMIF model
Isoform 1 of Rho guanine nucleotide exchange factor 2 DAMMIF model

Synchrotron SAXS data from solutions of N-terminal domain construct of hsGEFH1_190-582aa fit to DAMMIF and Alphafold2 models in 20mM Tris-Cl, 150mM NaCl, 1mM DTT, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). . The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Wavelength = UNKNOWN. Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN. Concentration = UNKNOWN

Isoform 1 of Rho guanine nucleotide exchange factor 2
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   46.7 kDa
 
UniProt   Q92974-1 (190-582)
Sequence   FASTA