Small-Angle X-ray Scattering data (benchmarking/consensus): EMBL-P12 SAXS beam line, DESY

Clement Blanchet, Melissa Graewert, Cy M Jeffries, Dmitri Svergun.

SASDPN7 – Xylanase SEC-WAXS data (EMBL-P12 bioSAXS beam line at DESY)

MWexperimental 21 kDa
MWexpected 21 kDa
VPorod 24 nm3
log I(s) 1.94×10-2 1.94×10-3 1.94×10-4 1.94×10-5
Endo-1,4-beta-xylanase small angle scattering data  s, nm-1
ln I(s)
Endo-1,4-beta-xylanase Guinier plot ln 1.94×10-2 Rg: 1.6 nm 0 (1.6 nm)-2 s2
Endo-1,4-beta-xylanase Kratky plot 1.104 0 3 sRg
Endo-1,4-beta-xylanase pair distance distribution function Rg: 1.6 nm 0 Dmax: 4.5 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Xylanase in 50 mM Tris, 100 mM NaCl, 1% v/v glycerol, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.062 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 75.00 μl sample at 8.6 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 75 Increase 10/300 column at 20°C. 24 successive 1 second frames were collected through the main SEC elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

The quoted experimental MW was determined from MALLS/RI data. The full entry .zip archive contains MW estimates from MALLS/UV and from I(0) and concentration in addition to the relative- and absolute-scaled unsubtracted SEC-SAXS data frames collected through the entire SEC-elution (2100 data frames), the CHROMIXS Rg-correlation through the SEC-elution peak, and the selected unsubtracted sample and buffer frames used to generate the profile displayed in this entry. These data form part of the 'Consensus and benchmarking SAS data project' by Trewhella et al., 2022:

Tags: benchmark
Mol. type   Protein
Organism   Trichoderma longibrachiatum
Olig. state   Monomer
Mon. MW   20.8 kDa
UniProt   F8W669 (1-190)
Sequence   FASTA