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

SASDET8 – GTPase Elongation Factor like-1 bound Shwachman-Diamond Syndrome protein (EFL1*SDo1)

Ribosome assembly protein 1
Ribosome maturation protein SDO1
MWexperimental 185 kDa
MWexpected 153 kDa
VPorod 333 nm3
log I(s) 4.73×10-2 4.73×10-3 4.73×10-4 4.73×10-5
Ribosome assembly protein 1 Ribosome maturation protein SDO1 small angle scattering data  s, nm-1
ln I(s)
Ribosome assembly protein 1 Ribosome maturation protein SDO1 Guinier plot ln 4.73×10-2 Rg: 5 nm 0 (5 nm)-2 s2
(sRg)2I(s)/I(0)
Ribosome assembly protein 1 Ribosome maturation protein SDO1 Kratky plot 1.104 0 3 sRg
p(r)
Ribosome assembly protein 1 Ribosome maturation protein SDO1 pair distance distribution function Rg: 4.7 nm 0 Dmax: 16 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Ribosome assembly protein 1 Ribosome maturation protein SDO1 DAMFILT model

Synchrotron SAXS data from solutions of GTPase Elongation Factor like-1 bound Shwachman-Diamond Syndrome protein (EFL1*SDo1) 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: 6.5 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
 
Ribosome maturation protein SDO1 (SDO1)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Monomer
Mon. MW   28.3 kDa
 
UniProt   Q07953
Sequence   FASTA