Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.

Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL, BMC Biol 16(1):76 (2018) Europe PMC

SASDDB6 – Small glutamine-rich tetratricopeptide repeat-containing protein alpha (full length; SGTA_FL)

Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length
MWexperimental 65 kDa
MWexpected 68 kDa
log I(s) 1.68×104 1.68×103 1.68×102 1.68×101
Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length small angle scattering data  s, nm-1
ln I(s)
Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length Guinier plot ln 1.69×104 Rg: 4.2 nm 0 (4.2 nm)-2 s2
(sRg)2I(s)/I(0)
Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length Kratky plot 1.104 0 3 sRg

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the small glutamine-rich tetratricopeptide repeat-containing protein alpha (full length; SGTA_FL) in 10 mM potassium phosphate, 100 mM NaCl, pH 6, were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY, 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). Solute concentrations ranging between 0.6 and 8.8 mg/ml were measured at 25°C. 20 successive 0.045 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Storage temperature = UNKNOWN

Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length (SGTA_FL)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   34.2 kDa
 
UniProt   O43765 (1-313)
Sequence   FASTA