Photosynthetic CO2 assimilation: the last gap in the structural proteome is closed

Alessandra Del Giudice.

SASDDH9 – Chloroplastic phosphoribulokinase (collected using SEC-SAXS)

Phosphoribulokinase, chloroplastic
MWI(0) 70 kDa
MWexpected 78 kDa
VPorod 115 nm3
log I(s) 4.20×101 4.20×100 4.20×10-1 4.20×10-2
Phosphoribulokinase, chloroplastic small angle scattering data  s, nm-1
ln I(s)
Phosphoribulokinase, chloroplastic Guinier plot ln 4.20×101 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoribulokinase, chloroplastic Kratky plot 1.104 0 3 sRg
p(r)
Phosphoribulokinase, chloroplastic pair distance distribution function Rg: 3.5 nm 0 Dmax: 11.3 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of chloroplastic phosphoribulokinase (collected using SEC-SAXS) in Tris-HCl 50 mM 150 mM KCl, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 4°C. 80 successive 1 second frames were collected through the SEC-elution profile. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank (eluate SEC-buffer) was subtracted.

Additional SEC parameters: Column type: Superdex 200 10/300 GL (GE Healthcare); Flow rate: 0.5 ml/min; Sample injection concentration: 6.1 mg/ml; Injection volume: 100 µl.

Phosphoribulokinase, chloroplastic (CrPRK)
Mol. type   Protein
Organism   Chlamydomonas reinhardtii
Olig. state   Dimer
Mon. MW   38.9 kDa
 
UniProt   P19824 (32-375)
Sequence   FASTA