UniProt ID: P51587 (1212-1551) Breast cancer type 2 susceptibility protein (BRC repeats 2-4)
UniProt ID: Q06609 (1-339) DNA repair protein RAD51 homolog 1 (F86E A89E)
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| Sample: |
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) monomer, 39 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) trimer, 111 kDa Homo sapiens protein
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| Buffer: |
20 mM Hepes, 350 mM KCl, 1 mM DTT, 5% Glycerol, pH: 7.5 |
| Experiment: |
SAXS
data collected at B21, Diamond Light Source on 2024 Dec 4
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Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination
(2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
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| RgGuinier |
6.9 |
nm |
| Dmax |
28.5 |
nm |
| VolumePorod |
652 |
nm3 |
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UniProt ID: P51587 (1212-1551) Breast cancer type 2 susceptibility protein (BRC repeats 2-4)
UniProt ID: Q06609 (1-339) DNA repair protein RAD51 homolog 1 (F86E A89E)
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| Sample: |
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) monomer, 39 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) trimer, 111 kDa Homo sapiens protein
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| Buffer: |
20 mM Hepes, 350 mM KCl, 1 mM DTT, 5% Glycerol, pH: 7.5 |
| Experiment: |
SAXS
data collected at B21, Diamond Light Source on 2024 Dec 4
|
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination
(2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
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| RgGuinier |
6.8 |
nm |
| Dmax |
28.3 |
nm |
| VolumePorod |
542 |
nm3 |
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UniProt ID: A0A0D1JF17 (1-109) Cyclic-di-AMP receptor
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| Sample: |
Cyclic-di-AMP receptor trimer, 42 kDa Staphylococcus aureus protein
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| Buffer: |
20 mM Tris, 150 mM NaCl, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2018 Dec 11
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Activation of a Secondary-Messenger Receptor via Allosteric Modulation of a Dynamic Conformational Ensemble.
Angew Chem Int Ed Engl :e202509394 (2025)
Söldner B, Singh H, Akoury E, Witte G, Linser R
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| RgGuinier |
2.7 |
nm |
| Dmax |
11.0 |
nm |
| VolumePorod |
91 |
nm3 |
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UniProt ID: A0A0D1JF17 (1-109) Cyclic-di-AMP receptor
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| Sample: |
Cyclic-di-AMP receptor trimer, 42 kDa Staphylococcus aureus protein
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| Buffer: |
20 mM Tris, 150 mM NaCl, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2018 Dec 11
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Activation of a Secondary-Messenger Receptor via Allosteric Modulation of a Dynamic Conformational Ensemble.
Angew Chem Int Ed Engl :e202509394 (2025)
Söldner B, Singh H, Akoury E, Witte G, Linser R
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| RgGuinier |
2.6 |
nm |
| Dmax |
11.0 |
nm |
| VolumePorod |
86 |
nm3 |
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UniProt ID: P0A6Y8 (None-None) Chaperone protein DnaK
UniProt ID: Q8IL04 (None-None) Heme ligase
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| Sample: |
Chaperone protein DnaK, 69 kDa Escherichia coli (strain … protein
Heme ligase, 28 kDa Plasmodium falciparum (isolate … protein
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| Buffer: |
20 mM Tris-Cl, 200 mM NaCl, pH: 8 |
| Experiment: |
SAXS
data collected at Anton Paar SAXSpace, Chemistry Division, Bhabha Atomic Research Centre on 2019 Feb 26
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Recombinant expression and purification of Plasmodium heme detoxification protein in E. coli: Challenges and discoveries.
Protein Expr Purif 236:106789 (2025)
Singh R, Makde RD
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| RgGuinier |
3.8 |
nm |
| Dmax |
13.8 |
nm |
| VolumePorod |
83 |
nm3 |
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UniProt ID: Q9UQM7 (7-478) Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ329-344)
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| Sample: |
Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ329-344) dodecamer, 620 kDa Homo sapiens protein
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| Buffer: |
50 mM Tris , 0.2 mM CaCl2, 150 mM KCl, 10 mM MgCl2, 2 mM ATP, pH: 8 |
| Experiment: |
SAXS
data collected at Rigaku/BioSAXS-2000 SAXS, Institute for Applied Life Sciences/Biophysical Characterization on 2024 Dec 18
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A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation - revision
Bao Nguyen Viet
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UniProt ID: Q9UQM7 (7-478) Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ329-344)
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| Sample: |
Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ329-344) dodecamer, 620 kDa Homo sapiens protein
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| Buffer: |
50 mM Tris , 0.2 mM CaCl2, 150 mM KCl, 10 mM MgCl2, 2 mM ATP, pH: 8 |
| Experiment: |
SAXS
data collected at Rigaku/BioSAXS-2000 SAXS, Institute for Applied Life Sciences/Biophysical Characterization on 2024 Dec 18
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A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation - revision
Bao Nguyen Viet
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UniProt ID: Q9UQM7 (7-478) Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ329-344)
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| Sample: |
Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ329-344) dodecamer, 620 kDa Homo sapiens protein
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| Buffer: |
50 mM Tris , 0.2 mM CaCl2, 150 mM KCl, 10 mM MgCl2, 2 mM ATP, pH: 8 |
| Experiment: |
SAXS
data collected at Rigaku/BioSAXS-2000 SAXS, Institute for Applied Life Sciences/Biophysical Characterization on 2024 Dec 18
|
A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation - revision
Bao Nguyen Viet
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UniProt ID: Q9UQM7 (7-478) Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ329-344)
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| Sample: |
Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ329-344) dodecamer, 620 kDa Homo sapiens protein
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| Buffer: |
50 mM Tris , 0.2 mM CaCl2, 150 mM KCl, 10 mM MgCl2, 2 mM ATP, pH: 8 |
| Experiment: |
SAXS
data collected at Rigaku/BioSAXS-2000 SAXS, Institute for Applied Life Sciences/Biophysical Characterization on 2024 Dec 18
|
A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation - revision
Bao Nguyen Viet
|
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UniProt ID: Q9UQM7 (7-478) Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ 316-329)
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| Sample: |
Calcium/calmodulin-dependent protein kinase type II subunit alpha (Δ1-6; Q223K; Δ 316-329) dodecamer, 626 kDa Homo sapiens protein
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| Buffer: |
50 mM Tris , 0.2 mM CaCl2, 150 mM KCl, 10 mM MgCl2, 2 mM ATP, pH: 8 |
| Experiment: |
SAXS
data collected at Rigaku/BioSAXS-2000 SAXS, Institute for Applied Life Sciences/Biophysical Characterization on 2024 Dec 18
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A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation - revision
Bao Nguyen Viet
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