OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.

Sluchanko NN, Slonimskiy YB, Shirshin EA, Moldenhauer M, Friedrich T, Maksimov EG, Nat Commun 9(1):3869 (2018) Europe PMC

SASDDE9 – Synechocystis fluorescence recovery protein FRPcc in the pre-oxidized state (CC mutant)

Fluorescence recovery protein
MWexperimental 27 kDa
MWexpected 28 kDa
VPorod 43 nm3
log I(s) 1.70×10-2 1.70×10-3 1.70×10-4 1.70×10-5
Fluorescence recovery protein small angle scattering data  s, nm-1
ln I(s)
Fluorescence recovery protein Guinier plot ln 1.70×10-2 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Fluorescence recovery protein Kratky plot 1.104 0 √3 sRg
p(r)
Fluorescence recovery protein pair distance distribution function Rg: 3.1 nm 0 Dmax: 13 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Fluorescence recovery protein CORAL model
Synchrotron SAXS data from solutions of Synechocystis fluorescence recovery protein FRPcc in the pre-oxidized state in 20 mM Tris-HCl, 150 mM NaCl, 0.1 mM EDTA, 3 % v/v glycerol, pH 7.6 were collected at the EMBL-P12 bioSAXS beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 1.7 mg/ml was measured at 10°C. 20 successive 0.050 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 and the data scaled for protein concentration.

Sample detector distance = UNKNOWN

Fluorescence recovery protein
Mol. type   Protein
Organism   Synechocystis sp. PCC 6803
Olig. state   Dimer
Mon. MW   14.1 kDa
 
UniProt   P74103
Sequence   FASTA