| MWexperimental | 46 | kDa |
| MWexpected | 52 | kDa |
| VPorod | 56 | nm3 |
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log I(s)
2.82×103
2.82×102
2.82×101
2.82×100
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s, nm-1
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Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.
Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K, PLoS One 15(12):e0242677 (2020) Europe PMCSASDGA7 – Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN1 repeats 7-15
Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN (7-15)|
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Fits and models
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Synchrotron SAXS
data from solutions of
Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN1 repeats 7-15
in
20 mM Tris-HCl, 200 mM NaCl, 2% (w/v) glycerol, 0.5 mM DTT, pH 8.5
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 m and
at a wavelength of λ = 0.124 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 100.00 μl sample
at 3.8 mg/ml was injected at a 0.50 ml/min flow rate
onto a GE Superdex 200 Increase 10/300 column
at 20°C.
60 successive
1 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.
Storage temperature = UNKNOWN |
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