X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism.

Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI, PLoS One 11(5):e0156105 (2016) Europe PMC

SASDBZ2 – Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli

Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli
MWI(0) 340 kDa
MWexpected 381 kDa
VPorod 484 nm3
log I(s) 1.68×104 1.68×103 1.68×102 1.68×101
Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli small angle scattering data  s, nm-1
ln I(s)
Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli Guinier plot ln 1.68×104 Rg: 4.4 nm 0 (4.4 nm)-2 s2
(sRg)2I(s)/I(0)
Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli Kratky plot 1.104 0 √3 sRg
p(r)
Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli pair distance distribution function Rg: 4.3 nm 0 Dmax: 12.7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli DAMMIN model
log I(s)
 s, nm-1
Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli CORAL model
Synchrotron SAXS data from solutions of Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli in 50 mM Tris pH 7.5 were collected on the P12 beam line of Petra-III (Hamburg, Germany) using a Pilatus 2M detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.124 nm). Different solute concentrations in the range 2.6-13.30 mg/ml were measured using an exposure time of 1 s (recorded as 20 x 0.050 s frames). The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering from the matched solvent-blank was subtracted. The data presented here are from a single concentration scattering curve (9.3 mg/ml).

The models displayed above are, from top to bottom: 1) An individual DAMMIN dummy atom model and; 2) CORAL rigid body model with the associated CRYSOL fit to the data. All of the individual DAMMIN models and associated fits can be found in the zip archive for this entry along with the CORAL modelling results.

Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli (FbaB)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Decamer
Mon. MW   38.1 kDa
 
UniProt   A0A0K4BP99
Sequence   FASTA