Magnetic field effects on the structure and molecular behavior of pigeon iron–sulfur protein

Arai S, Shimizu R, Adachi M, Hirai M, Protein Science 31(6) (2022) DOI

SASDLL8 – The Fe–S cluster assembly 1 homolog of pigeon (retention time at the magnet position No.5 : 10 min)

Iron-sulfur cluster assembly 1 homolog, mitochondrial
MWexperimental 457 kDa
MWexpected 15 kDa
log I(s) 3.33×10-1 3.33×10-2 3.33×10-3 3.33×10-4
Iron-sulfur cluster assembly 1 homolog, mitochondrial small angle scattering data  s, nm-1
ln I(s)
Iron-sulfur cluster assembly 1 homolog, mitochondrial Guinier plot ln 3.34×10-1 Rg: 5.7 nm 0 (5.7 nm)-2 s2
(sRg)2I(s)/I(0)
Iron-sulfur cluster assembly 1 homolog, mitochondrial Kratky plot 1.104 0 3 sRg
p(r)
Iron-sulfur cluster assembly 1 homolog, mitochondrial pair distance distribution function Rg: 5.1 nm 0 Dmax: 18.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of The Fe–S cluster assembly 1 homolog of pigeon (retention time at the magnet position No.5 : 10 min) in 20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH 8 were collected on the BL-10C beam line at the Photon Factory (PF), High Energy Accelerator Research Organization (KEK) storage ring (Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.155 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). at 20°C. One 60 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

SAXS/WAXS data were measured at 20°C from a sample at 29.3 mg/ml using two different sample-to-detector distances (0.3 and 3 m), and merged using the program ATSAS 3.0.3. The sample solution was set at the position No. 5 in the periodic Nd-Fe-B permanent magnetic circuit [M. Hirai, M. Koizumi, R. Han, T. Hayakawa, Y. Sano, Right- /left-circular orientation of biological macromolecules under magnetic field gradient. J. Appl. Crystallogr. 36, 520–524 (2003)]. The retention time of a sample solution at the position No.5 in the magnet circuit was 10 min. P(r) was calculated from s = 0.16 to 5.18 nm-1.

Iron-sulfur cluster assembly 1 homolog, mitochondrial (clISCA1)
Mol. type   Protein
Organism   Columba livia
Olig. state   Unknown
Mon. MW   14.7 kDa
 
UniProt   P0DN75 (2-132)
Sequence   FASTA