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