| MWexperimental | 62 | kDa |
| MWexpected | 77 | kDa |
| VPorod | 104 | nm3 |
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log I(s)
2.66×10-2
2.66×10-3
2.66×10-4
2.66×10-5
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s, nm-1
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Structure and dynamics of UBA5-UFM1 complex formation showing new insights in the UBA5 activation mechanism
Fuchs S, Kikhney A, Schubert R, Kaiser C, Liebau E, Svergun D, Betzel C, Perbandt M, Journal of Structural Biology :107796 (2021) DOISASDLC3 – Ubiquitin activating enzyme 5 with ubiquitin-fold modifier 1 (UBA5 7 mg/mL + UFM1 1.75 mg/mL)
Ubiquitin-like modifier-activating enzyme 5Ubiquitin fold modifer 1
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Fits and models
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Synchrotron SAXS
data from solutions of
Ubiquitin activating enzyme 5 with ubiquitin-fold modifier 1 (UBA5 7 mg/mL + UFM1 1.75 mg/mL)
in
20 mM Tris, 50 mM NaCl, 2 mM DTT, pH 7.5
were collected
on the
EMBL P12 beam line
at the PETRA III storage ring
(DESY; Hamburg, Germany)
using a Pilatus 6M detector
at a sample-detector distance of 3 m and
at a wavelength of λ = 0.123975 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 7.00 mg/ml was measured
at 20°C.
31 successive
0.100 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.
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