| MWexperimental | 32 | kDa |
| MWexpected | 28 | kDa |
| VPorod | 36 | nm3 |
|
log I(s)
2.05×102
2.05×101
2.05×100
2.05×10-1
|
s, nm-1
|
Structural and biochemical characterization of the C‐terminal region of the human RTEL
1 helicase
Cortone G,
Graewert M,
Kanade M,
Longo A,
Hegde R,
González‐Magaña A,
Chaves‐Arquero B,
Blanco F,
Napolitano L,
Onesti S,
Protein Science
33(9)
(2024)
DOISASDRW9 – Regulator of telomere elongation helicase 1, HHD1-HHD2 fragment
Regulator of telomere elongation helicase 1 (Isoform 6, 889-1147)|
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Fits and models
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Rg, nm
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Synchrotron SAXS
data from solutions of
Regulator of telomere elongation helicase 1, HHD1-HHD2 fragment
in
50 mM Hepes, 150 mM NaCl,10 (v/v)% glycerol, 1 mM TCEP, pH 7
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 4 m and
at a wavelength of λ = 0.154 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 40.00 μl sample
at 7.2 mg/ml was injected at a 0.20 ml/min flow rate
onto a GE Superdex 75 Increase 5/150 column
at 20°C.
2400 successive
0.500 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.
Dmax appears underestimated. Additional EOM .pdb coordinate/model files are provided in the full entry zip archive. |
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