Iron and redox sensing in plants: properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins

Julia Mundy.

SASDU79 – BRUTUS-LIKE2 N-Terminal Region (BTSL2-N)

Zinc finger protein BRUTUS-like At1g18910
MWexperimental 101 kDa
MWexpected 98 kDa
VPorod 162 nm3
log I(s) 6.16×10-2 6.16×10-3 6.16×10-4 6.16×10-5
Zinc finger protein BRUTUS-like At1g18910 small angle scattering data  s, nm-1
ln I(s)
Zinc finger protein BRUTUS-like At1g18910 Guinier plot ln 6.16×10-2 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
Zinc finger protein BRUTUS-like At1g18910 Kratky plot 1.104 0 √3 sRg
p(r)
Zinc finger protein BRUTUS-like At1g18910 pair distance distribution function Rg: 3.4 nm 0 Dmax: 9.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Zinc finger protein BRUTUS-like At1g18910 ALPHAFOLD model
Synchrotron SAXS data from solutions of BRUTUS-LIKE2 N-Terminal Region (BTSL2-N) in 10 mM MES, 15 mM NaCl, pH 6.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.09464 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 60.00 μl sample at 5 mg/ml was injected at a 0.07 ml/min flow rate onto a GE Superdex 200 Increase 3.2/300 column at 15°C. 600 successive 3 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.

Zinc finger protein BRUTUS-like At1g18910 (BTSL2-N)
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Monomer
Mon. MW   97.8 kDa
 
UniProt   F4IDY5 (1-831)
Sequence   FASTA