X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum.

Goettig P, Brandstetter H, Groll M, Göhring W, Konarev PV, Svergun DI, Huber R, Kim JS, J Biol Chem 280(39):33387-96 (2005) Europe PMC

SASDLQ5 – Tricorn protease oligomers

Tricorn protease
MWexperimental 380 kDa
MWexpected 730 kDa
log I(s) 2.57×103 2.57×102 2.57×101 2.57×100
Tricorn protease small angle scattering data  s, nm-1
ln I(s)
Tricorn protease Guinier plot ln 2.57×103 Rg: 5.9 nm 0 (5.9 nm)-2 s2
Tricorn protease Kratky plot 1.104 0 3 sRg

Data validation

Fits and models

log I(s)
 s, nm-1
Tricorn protease PDB (PROTEIN DATA BANK) model
Tricorn protease PDB (PROTEIN DATA BANK) model
Tricorn protease PDB (PROTEIN DATA BANK) model

Synchrotron SAXS data from solutions of tricorn protease oligomers in 20mM Tris-HCl, 100 mM NaCl, pH 7.5 were collected on the EMBL X33 beam line at DORIS III (DESY, Hamburg, Germany) using a 1D Gas detector detector at a sample-detector distance of 2.2 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 10.00 mg/ml was measured at 20°C. 10 successive 60 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.

Tags: X33
Tricorn protease (Tricorn)
Mol. type   Protein
Organism   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Olig. state   Hexamer
Mon. MW   121.6 kDa
UniProt   P96086 (1-1071)
Sequence   FASTA
PDB ID   1K32
PDB ID   1K32
PDB ID   1K32