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

SASDCG6 – EAL/GGDEF domain protein from M. capsulatus, Northeast Structural Genomics Consortium Target McR174C

EAL/GGDEF domain protein
MWexperimental 20 kDa
MWexpected 19 kDa
VPorod 34 nm3
log I(s) 9.33×102 9.33×101 9.33×100 9.33×10-1
EAL/GGDEF domain protein small angle scattering data  s, nm-1
ln I(s)
EAL/GGDEF domain protein Guinier plot ln 9.33×102 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
EAL/GGDEF domain protein Kratky plot 1.104 0 √3 sRg
p(r)
EAL/GGDEF domain protein pair distance distribution function Rg: 1.9 nm 0 Dmax: 6.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
EAL/GGDEF domain protein PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
EAL/GGDEF domain protein DAMFILT model
Synchrotron SAXS data from solutions of EAL/GGDEF domain protein from M. capsulatus, Northeast Structural Genomics Consortium Target McR174C 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 2.8 and 5.1 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.

EAL/GGDEF domain protein
Mol. type   Protein
Organism   Methylococcus capsulatus
Olig. state   Monomer
Mon. MW   18.8 kDa
 
UniProt   Q60BX6
Sequence   FASTA
 
PDB ID   3ICL