Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation.

Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK, Nucleic Acids Res 41(17):8166-81 (2013) Europe PMC

SASDAX3 – MutS tetramer

DNA mismatch repair protein MutS
MWexperimental 340 kDa
MWexpected 381 kDa
VPorod 750 nm3
log I(s) 3.01×102 3.01×101 3.01×100 3.01×10-1
DNA mismatch repair protein MutS small angle scattering data  s, nm-1
ln I(s)
DNA mismatch repair protein MutS Guinier plot ln 3.01×102 Rg: 8.5 nm 0 (8.5 nm)-2 s2
DNA mismatch repair protein MutS Kratky plot 1.104 0 3 sRg
DNA mismatch repair protein MutS pair distance distribution function 0 Dmax: 29 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of MutS tetramer in 50 mM HEPES 50 mM KCl, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 2M detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.86 mg/ml was measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Wavelength = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Tags: X33
DNA mismatch repair protein MutS (MutS tetramer)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Tetramer
Mon. MW   95.3 kDa
UniProt   P23909
Sequence   FASTA