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

SASDCB6 – Nmul_A1745 protein from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR72

Uncharacterized protein
MWexperimental 50 kDa
MWexpected 55 kDa
VPorod 83 nm3
log I(s) 1.72×102 1.72×101 1.72×100 1.72×10-1
Uncharacterized protein small angle scattering data  s, nm-1
ln I(s)
Uncharacterized protein Guinier plot ln 1.72×102 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
Uncharacterized protein Kratky plot 1.104 0 √3 sRg
p(r)
Uncharacterized protein pair distance distribution function Rg: 2.3 nm 0 Dmax: 7.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Uncharacterized protein DAMFILT model
log I(s)
 s, nm-1
Uncharacterized protein PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Nmul_A1745 protein from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR72 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 0.7 and 2.2 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.

Uncharacterized protein
Mol. type   Protein
Organism   Nitrosospira multiformis
Olig. state   Tetramer
Mon. MW   13.7 kDa
 
UniProt   Q2Y879
Sequence   FASTA
 
PDB ID   3LMF