Heterologous Expression and Biochemical Characterization of the Human Zinc Transporter 1 (ZnT1) and Its Soluble C-Terminal Domain

Cotrim C, Jarrott R, Whitten A, Choudhury H, Drew D, Martin J, Frontiers in Chemistry 9 (2021) DOI

SASDJ85 – Zinc transporter 1 – hZnT1-CTD

Zinc transporter 1
MWexperimental 41 kDa
MWexpected 37 kDa
VPorod 50 nm3
log I(s) 5.93×10-3 5.93×10-4 5.93×10-5 5.93×10-6
Zinc transporter 1 small angle scattering data  s, nm-1
ln I(s)
Zinc transporter 1 Guinier plot ln 5.93×10-3 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Zinc transporter 1 Kratky plot 1.104 0 √3 sRg
p(r)
Zinc transporter 1 pair distance distribution function Rg: 2.8 nm 0 Dmax: 10 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Zinc transporter 1 DAMFILT model
log I(s)
 s, nm-1
Zinc transporter 1 CORAL model
X-ray synchrotron radiation scattering data from solutions of the soluble C-terminal domain of human zinc transporter-1 (ZnT1) in 20 mM Tris 150mM NaCl, 1mM NaCl, pH 7.6 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 2M pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). The sample was measured in an in-line SEC-SEXS configuration with sheath flow in the capilary to reduce radiation damage. Thirty successive 1 second frames were collected across the elution peak, where the average protein concentration is estimated to be ~0.2 mg/mL (but the A280 was not measured as the protein eluted). The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The models and corresponding fits include those derived from dummy atom modelling using DAMMIN (top) and rigid-body modelling using CORAL (bottom).

SEC column = UNKNOWN. Sample injection volume = UNKNOWN. Flow rate = UNKNOWN

Zinc transporter 1 (ZnT1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   18.3 kDa
 
UniProt   Q9Y6M5 (342-507)
Sequence   FASTA