Small angle X-ray scattering as a complementary tool for high-throughput structural studies.

Grant TD, Luft JR, Wolfley JR, Tsuruta H, Martel A, Montelione GT, Snell EH, Biopolymers 95(8):517-30 (2011) Europe PMC

SASDCJ6 – MmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G

MmoQ
MWexperimental 37 kDa
MWexpected 32 kDa
VPorod 62 nm3
log I(s) 1.01×103 1.01×102 1.01×101 1.01×100
MmoQ small angle scattering data  s, nm-1
ln I(s)
MmoQ Guinier plot ln 1.02×103 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
MmoQ Kratky plot 1.104 0 √3 sRg
p(r)
MmoQ pair distance distribution function Rg: 2.3 nm 0 Dmax: 8.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
MmoQ PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
MmoQ DAMFILT model
Synchrotron SAXS data from solutions of MmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G in 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3, pH 7.5 were collected on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (SSRL) storage ring (Menlo Park, CA, USA) using a Rayonix MX225-HE detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.13 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2.5 and 5.3 mg/ml were measured at 20°C. 20 successive 1 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.

MmoQ
Mol. type   Protein
Organism   Methylococcus capsulatus
Olig. state   Monomer
Mon. MW   32.0 kDa
 
UniProt   Q7WZ31
Sequence   FASTA
 
PDB ID   3IGN