Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga Chlamydomonas reinhardtii.

Charoenwattanasatien R, Zinzius K, Scholz M, Wicke S, Tanaka H, Brandenburg JS, Marchetti GM, Ikegami T, Matsumoto T, Oda T, Sato M, Hippler M, Kurisu G, J Biol Chem (2019) Europe PMC

SASDE99 – Calredoxin with EGTA

Calredoxin, Redox protein from Chlamydomonas reinhardtii
MWexperimental 33 kDa
MWexpected 40 kDa
VPorod 60 nm3
log I(s) 5.80×10-1 5.80×10-2 5.80×10-3 5.80×10-4
Calredoxin, Redox protein from Chlamydomonas reinhardtii small angle scattering data  s, nm-1
ln I(s)
Calredoxin, Redox protein from Chlamydomonas reinhardtii Guinier plot ln 5.80×10-1 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Calredoxin, Redox protein from Chlamydomonas reinhardtii Kratky plot 1.104 0 √3 sRg
p(r)
Calredoxin, Redox protein from Chlamydomonas reinhardtii pair distance distribution function Rg: 2.5 nm 0 Dmax: 8.7 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of Calredoxin with EGTA in 20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM EGTA, pH 8 were collected on a Rigaku BioSAXS-1000 instrument at the Structural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University (Yokohama, Japan) using a Pilatus 100K detector at a wavelength of λ = 0.15418 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 20°C. Two successive 120 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.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Calredoxin, Redox protein from Chlamydomonas reinhardtii (CRX)
Mol. type   Protein
Organism   Chlamydomonas reinhardtii
Olig. state   Monomer
Mon. MW   39.9 kDa
 
UniProt   A0A2K3DZB3 (25-357)
Sequence   FASTA