Radiation resistivity of clISCA1

Shigeki Arai.

SASDLX7 – The Fe–S cluster assembly 1 homolog of pigeon (29.3 mg/ml), Total X-ray exposure time : 5min

Iron-sulfur cluster assembly 1 homolog, mitochondrial
MWexperimental 471 kDa
MWexpected 15 kDa
log I(s) 3.41×10-1 3.41×10-2 3.41×10-3 3.41×10-4
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 3.41×10-1 Rg: 4.4 nm 0 (4.4 nm)-2 s2
(sRg)2I(s)/I(0)
Iron-sulfur cluster assembly 1 homolog, mitochondrial Kratky plot 1.104 0 3 sRg

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 (29.3 mg/ml), Total X-ray exposure time : 5min 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 exposure time to collect I(q) was 1 min. This sample was measured after 4 min X-ray exposure to check the radiation damage.

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