Interaction of the GTPase Elongation Factor Like-1 with the Shwachman-Diamond Syndrome Protein and Its Missense Mutations.

Gijsbers A, Montagut DC, Méndez-Godoy A, Altamura D, Saviano M, Siliqi D, Sánchez-Puig N, Int J Mol Sci 19(12) (2018) Europe PMC

SASDEU8 – GTPase Elongation Factor like-1 protein (yeast EFL1)

Ribosome assembly protein 1
MWexperimental 169 kDa
MWexpected 124 kDa
VPorod 258 nm3
log I(s) 7.50×10-2 7.50×10-3 7.50×10-4 7.50×10-5
Ribosome assembly protein 1 small angle scattering data  s, nm-1
ln I(s)
Ribosome assembly protein 1 Guinier plot ln 7.50×10-2 Rg: 4.7 nm 0 (4.7 nm)-2 s2
Ribosome assembly protein 1 Kratky plot 1.104 0 3 sRg
Ribosome assembly protein 1 pair distance distribution function Rg: 4.6 nm 0 Dmax: 15.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Ribosome assembly protein 1 DAMFILT model

log I(s)
 s, nm-1
Ribosome assembly protein 1 MULTIFOXS model
Ribosome assembly protein 1 MULTIFOXS model
Ribosome assembly protein 1 MULTIFOXS model

Synchrotron SAXS data from solutions of GTPase Elongation Factor like-1 protein (yeast EFL1) in 50 mM Tris pH 8.0, 10% glycerol, 300 mM NaCl and 5 mM MgCl2., pH 8 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the B21 camera at the Diamond Light Source storage ring (Oxfordshire, UK) using a Pilatus 2M detector at a sample-detector distance of 3.0 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). The data obtained through the sample elution peak (collected as 580 successive 3 second frames) were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the individual subtracted data sets were scaled and averaged to generate the scattering profile displayed in this entry.

SEC-SAXS was performed at 20°C using the following parameters: Column: Shodex KW-403 ; Flow rate: 0.408 mL/min; Total acquisition time: 1740s; Sample injection concentration: 10 mg/mL; Injection volume: 45μL

Ribosome assembly protein 1 (EFL1)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Monomer
Mon. MW   124.5 kDa
UniProt   P53893
Sequence   FASTA