The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility.

Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV, Nat Microbiol (2019) Europe PMC

SASDEU7 – Stator protein FlaG soluble domain

Conserved flagellar protein FlaG soluble domain
MWexperimental 24 kDa
MWexpected 15 kDa
VPorod 133 nm3
log I(s) 4.64×101 4.64×100 4.64×10-1 4.64×10-2
Conserved flagellar protein FlaG soluble domain small angle scattering data  s, nm-1
ln I(s)
Conserved flagellar protein FlaG soluble domain Guinier plot ln 4.64×101 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Conserved flagellar protein FlaG soluble domain Kratky plot 1.104 0 3 sRg
p(r)
Conserved flagellar protein FlaG soluble domain pair distance distribution function Rg: 4.4 nm 0 Dmax: 18 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the stator protein FlaG soluble domain in 25 mM citric acid/sodium citrate, 150mM NaCl, 3% glycerol, pH 3 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.127 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.5 and 5 mg/ml were measured at 10°C. 33 successive 0.300 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

Conserved flagellar protein FlaG soluble domain (sFlaG)
Mol. type   Protein
Organism   Sulfolobus acidocaldarius
Olig. state   Monomer
Mon. MW   14.9 kDa
 
UniProt   Q4J9K7 (32-151)
Sequence   FASTA