The structure and flexibility analysis of the Arabidopsis
synaptotagmin 1 reveal the basis of its regulation at membrane contact sites
Benavente J,
Siliqi D,
Infantes L,
Lagartera L,
Mills A,
Gago F,
Ruiz-López N,
Botella M,
Sánchez-Barrena M,
Albert A
Life Science Alliance
4(10):e202101152
(2021 Aug 18)
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Sample: |
Synaptotagmin-1 monomer, 33 kDa Arabidopsis thaliana protein
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Buffer: |
50 mM Tris, 50 mM NaCl, pH: 8 |
Experiment: |
SAXS
data collected at B21, Diamond Light Source on 2020 Jun 11
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RgGuinier |
3.1 |
nm |
Dmax |
12.1 |
nm |
VolumePorod |
59 |
nm3 |
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Sample: |
Synaptotagmin-1 (SYT1-SMP2C2A) monomer, 72 kDa Escherichia coli protein
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Buffer: |
20 mM Tris, 100 mM NaCl, 5% glycerol, 2 mM DTT, pH: 8 |
Experiment: |
SAXS
data collected at B21, Diamond Light Source on 2020 Jun 11
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RgGuinier |
4.2 |
nm |
Dmax |
17.8 |
nm |
VolumePorod |
138 |
nm3 |
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Sample: |
Synaptotagmin-1 monomer, 33 kDa Arabidopsis thaliana protein
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Buffer: |
50 mM Tris, 50 mM NaCl, pH: 8 |
Experiment: |
SAXS
data collected at B21, Diamond Light Source on 2021 Feb 16
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RgGuinier |
2.8 |
nm |
Dmax |
12.6 |
nm |
VolumePorod |
50 |
nm3 |
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Sample: |
Synaptotagmin-1 monomer, 33 kDa Arabidopsis thaliana protein
|
Buffer: |
50 mM Tris, 50 mM NaCl, pH: 8 |
Experiment: |
SAXS
data collected at B21, Diamond Light Source on 2021 Feb 16
|
|
RgGuinier |
2.9 |
nm |
Dmax |
13.8 |
nm |
VolumePorod |
54 |
nm3 |
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