UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
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Sample: |
Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
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Buffer: |
20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8 |
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Nov 30
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Radiation resistivity of clISCA1
Shigeki Arai
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UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
|
|
|
Sample: |
Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
|
Buffer: |
20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8 |
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Nov 30
|
Radiation resistivity of clISCA1
Shigeki Arai
|
|
|
UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
|
|
|
Sample: |
Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
|
Buffer: |
20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8 |
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2021 Jun 8
|
Radiation resistivity of clISCA1
Shigeki Arai
|
|
|
UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
|
|
|
Sample: |
Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
|
Buffer: |
20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8 |
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2021 Jun 8
|
Radiation resistivity of clISCA1
Shigeki Arai
|
|
|
UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
|
|
|
Sample: |
Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
|
Buffer: |
20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8 |
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2021 Jun 8
|
Radiation resistivity of clISCA1
Shigeki Arai
|
|
|
UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
|
|
|
Sample: |
Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
|
Buffer: |
20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8 |
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2021 Jun 8
|
Radiation resistivity of clISCA1
Shigeki Arai
|
|
|
UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
|
|
|
Sample: |
Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
|
Buffer: |
20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8 |
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2021 Jun 8
|
Radiation resistivity of clISCA1
Shigeki Arai
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UniProt ID: Q9UK39 (68-431) Nocturnin
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Sample: |
Nocturnin monomer, 41 kDa Homo sapiens protein
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Buffer: |
50 mM HEPES, 150 mM KCl, 10% glycerol, 5 mM MgCl2, 1 mM TCEP, pH: 7.5 |
Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Feb 7
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The Disordered Amino Terminus of the Circadian Enzyme Nocturnin Modulates Its NADP(H) Phosphatase Activity by Changing Protein Dynamics.
Biochemistry (2022)
Wickramaratne AC, Li L, Hopkins JB, Joachimiak LA, Green CB
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RgGuinier |
2.9 |
nm |
Dmax |
12.3 |
nm |
VolumePorod |
85 |
nm3 |
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UniProt ID: Q9UK39 (68-431) Nocturnin
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Sample: |
Nocturnin monomer, 41 kDa Homo sapiens protein
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Buffer: |
50 mM HEPES, 150 mM KCl, 10% glycerol, 5 mM MgCl2, 1 mM TCEP, pH: 7.5 |
Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Feb 7
|
The Disordered Amino Terminus of the Circadian Enzyme Nocturnin Modulates Its NADP(H) Phosphatase Activity by Changing Protein Dynamics.
Biochemistry (2022)
Wickramaratne AC, Li L, Hopkins JB, Joachimiak LA, Green CB
|
RgGuinier |
2.4 |
nm |
Dmax |
9.6 |
nm |
VolumePorod |
76 |
nm3 |
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UniProt ID: Q9UK39 (None-None) Nocturnin - Deletion construct - Δ107-120
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Sample: |
Nocturnin - Deletion construct - Δ107-120 monomer, 40 kDa protein
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Buffer: |
50 mM HEPES, 150 mM KCl, 10% glycerol, 5 mM MgCl2, 1 mM TCEP, pH: 7.5 |
Experiment: |
SAXS
data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Feb 7
|
The Disordered Amino Terminus of the Circadian Enzyme Nocturnin Modulates Its NADP(H) Phosphatase Activity by Changing Protein Dynamics.
Biochemistry (2022)
Wickramaratne AC, Li L, Hopkins JB, Joachimiak LA, Green CB
|
RgGuinier |
2.8 |
nm |
Dmax |
11.2 |
nm |
VolumePorod |
72 |
nm3 |
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