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

SASDEW8 – Shwachman-Bodian-Diamond Syndrome protein (SDO1) with domains 2 and 3

Ribosome maturation protein SDO1
MWexperimental 18 kDa
MWexpected 17 kDa
VPorod 25 nm3
log I(s) 1.18×103 1.18×102 1.18×101 1.18×100
Ribosome maturation protein SDO1 small angle scattering data  s, nm-1
ln I(s)
Ribosome maturation protein SDO1 Guinier plot ln 1.18×103 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Ribosome maturation protein SDO1 Kratky plot 1.104 0 3 sRg
p(r)
Ribosome maturation protein SDO1 pair distance distribution function Rg: 2.0 nm 0 Dmax: 6.2 nm

Data validation


Fits and models


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

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

Synchrotron SAXS data from solutions of Shwachman-Bodian-Diamond Syndrome protein (SDO1) with domains 2 and 3 in 50 mM Tris pH 8.0, 10% glycerol, 300 mM NaCl and 5 mM MgCl2, pH 8 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 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 successive 1 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 (using FPLC–Malvern TDA system ) was performed at 20°C using the following parameters: Column: Superdex 200 Increase 10/300GL ; Flow rate: 0.4 mL/min; Total acquisition time: 1850s; Sample injection concentration: 15 mg/mL; Injection volume: 50μL.

Ribosome maturation protein SDO1 (SDO1_12)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Monomer
Mon. MW   17.5 kDa
 
UniProt   Q07953 (1-250)
Sequence   FASTA