Machine Learning Methods for X-Ray Scattering Data Analysis from Biomacromolecular Solutions.

Franke D, Jeffries CM, Svergun DI, Biophys J 114(11):2485-2492 (2018) Europe PMC

SASDDL3 – Folded ribonuclease A (RNAse)

Ribonuclease pancreatic

MW^I(0)	17	kDa
MW^expected	16	kDa
V^Porod	16	nm³

log I(s) 6.29×10² 6.29×10¹ 6.29×10⁰ 6.29×10^-1

Ribonuclease pancreatic small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 6.30×10² R_g: 1.6 nm 0 (1.6 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 1.6 nm 0 D_max: 5.6 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.2

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.816
1.042

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Ribonuclease pancreatic PDB (PROTEIN DATA BANK) model

Synchrotron SAXS data from solutions of Folded ribonuclease A (RNAse) in phosphate buffered saline (PBS), pH 7 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.24 mg/ml was measured at 10°C. Two successive 0.050 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.

Ribonuclease pancreatic (RNase)
Mol. type		Protein
Organism		Bos taurus
Olig. state		Monomer
Mon. MW		16.5 kDa

UniProt		P61823
Sequence		FASTA

PDB ID		3MZQ