Structure and dynamics of the von Willebrand Factor C6 domain

Chen P, Kutzki F, Mojzisch A, Simon B, Xu E, Aponte-Santamaría C, Horny K, Jeffries C, Schneppenheim R, Wilmanns M, Brehm M, Gräter F, Hennig J, Journal of Structural Biology 214(4):107923 (2022) DOI

SASDLQ9 – Von Willebrand Factor C6 domain wildtype

von Willebrand factor C6 domain wild type
MWexperimental 9 kDa
MWexpected 9 kDa
VPorod 12 nm3
log I(s) 1.26×103 1.26×102 1.26×101 1.26×100
von Willebrand factor C6 domain wild type small angle scattering data  s, nm-1
ln I(s)
von Willebrand factor C6 domain wild type Guinier plot ln 1.27×103 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
von Willebrand factor C6 domain wild type Kratky plot 1.104 0 3 sRg
p(r)
von Willebrand factor C6 domain wild type pair distance distribution function Rg: 1.8 nm 0 Dmax: 6.6 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Von Willebrand Factor C6 domain, wildtype, in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (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 4.56 mg/ml was measured at 20°C. 30 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.

von Willebrand factor C6 domain wild type (VWFC6 wt)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   8.7 kDa
 
UniProt   P04275 (2647-2720)
Sequence   FASTA