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

SASDDK3 – Candida antarctica lipase B - with guanidine-HCl unfolding series, in the presence of dithiothreitol

Lipase B from Pseudozyma antarctica
MWI(0) 35 kDa
MWexpected 33 kDa
log I(s) 1.26×103 1.26×102 1.26×101 1.26×100
Lipase B from Pseudozyma antarctica small angle scattering data  s, nm-1
ln I(s)
Lipase B from Pseudozyma antarctica Guinier plot ln 1.27×103 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Lipase B from Pseudozyma antarctica Kratky plot 1.104 0 √3 sRg

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Candida antarctica lipase B - with a guanidine-HCl unfolding series under reducing conditions - in 100 mM NaCl, 20 mM Na2HPO4, 10 mM DTT, pH 6, 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 (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.65 mg/ml was measured at 10°C. 29 successive 0.030 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.

In addition to the SAXS profile displayed above, two lipase B unfolding series in the presence of DTT spanning 0 M to 6 M guanidine hydrochloride are included in the full entry zip archive.

Lipase B from Pseudozyma antarctica (lipase B)
Mol. type   Protein
Organism   Moesziomyces antarcticus
Olig. state   Other
Mon. MW   33.0 kDa
 
UniProt   P41365 (26-342)
Sequence   FASTA