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29 hits found for Gabriele Giachin

SASDNF2 – Serine/threonine-protein phosphatase (PP1) bound to Protein phosphatase 1 (PTG)

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitProtein phosphatase 1 regulatory subunit 3C experimental SAS data
DAMMIF model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 37 kDa Homo sapiens protein
Protein phosphatase 1 regulatory subunit 3C monomer, 23 kDa Homo sapiens protein
Buffer: 50 mM Tris pH 8.0, 0.5 M NaCl, 10% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 7
Molecular architecture of the glycogen- committed PP1/PTG holoenzyme. Nat Commun 13(1):6199 (2022)
...Giachin G, Covaceuszach S, Cassetta A, Demitri N, Storici P, Lolli G
RgGuinier 3.3 nm
Dmax 11.9 nm
VolumePorod 87 nm3

SASDNG2 – Serine/threonine-protein phosphatase (PP1) bound to Protein phosphatase 1 (PTG) and cyclodextrin

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitProtein phosphatase 1 regulatory subunit 3C experimental SAS data
DAMFILT model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 37 kDa Homo sapiens protein
Protein phosphatase 1 regulatory subunit 3C monomer, 23 kDa Homo sapiens protein
Buffer: 50 mM Tris pH 8.0, 0.5 M NaCl, 10% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 7
Molecular architecture of the glycogen- committed PP1/PTG holoenzyme. Nat Commun 13(1):6199 (2022)
...Giachin G, Covaceuszach S, Cassetta A, Demitri N, Storici P, Lolli G
RgGuinier 3.6 nm
Dmax 12.3 nm
VolumePorod 89 nm3

SASDHU4 – ECSIT C-terminal domain

Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial experimental SAS data
DAMMIN model
Sample: Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial dimer, 44 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Dec 7
Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angew Chem Int Ed Engl (2020)
Giachin G, Jessop M, Bouverot R, Acajjaoui S, Saidi M, Chretien A, Bacia-Verloop M, Signor L, Mas PJ, Favier A, Borel Meneroud E, Hons M, Hart DJ, Kandiah E, Boeri Erba E, Buisson A, Leonard G, Gutsch...
RgGuinier 3.7 nm
Dmax 11.9 nm
VolumePorod 117 nm3

SASDHV4 – Mitochondrial complex I assembly factor, NDUFAF1

Complex I intermediate-associated protein 30, mitochondrial experimental SAS data
DAMMIN model
Sample: Complex I intermediate-associated protein 30, mitochondrial monomer, 35 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 29
Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angew Chem Int Ed Engl (2020)
Giachin G, Jessop M, Bouverot R, Acajjaoui S, Saidi M, Chretien A, Bacia-Verloop M, Signor L, Mas PJ, Favier A, Borel Meneroud E, Hons M, Hart DJ, Kandiah E, Boeri Erba E, Buisson A, Leonard G, Gutsch...
RgGuinier 3.3 nm
Dmax 9.6 nm
VolumePorod 82 nm3

SASDHW4 – Mitochondrial Complex I assembly factor, ACAD9

Complex I assembly factor ACAD9, mitochondrial experimental SAS data
DAMMIN model
Sample: Complex I assembly factor ACAD9, mitochondrial dimer, 132 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 28
Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angew Chem Int Ed Engl (2020)
Giachin G, Jessop M, Bouverot R, Acajjaoui S, Saidi M, Chretien A, Bacia-Verloop M, Signor L, Mas PJ, Favier A, Borel Meneroud E, Hons M, Hart DJ, Kandiah E, Boeri Erba E, Buisson A, Leonard G, Gutsch...
RgGuinier 3.6 nm
Dmax 10.2 nm
VolumePorod 217 nm3

SASDHX4 – Mitochondrial complex I assembly factor, ACAD9, chimeric construct where segment 445-482 has been replaced with segment 481-518 of VLCAD protein

Complex I assembly factor ACAD9-VLCAD chimera experimental SAS data
DAMFILT model
Sample: Complex I assembly factor ACAD9-VLCAD chimera dimer, 131 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Nov 30
Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angew Chem Int Ed Engl (2020)
Giachin G, Jessop M, Bouverot R, Acajjaoui S, Saidi M, Chretien A, Bacia-Verloop M, Signor L, Mas PJ, Favier A, Borel Meneroud E, Hons M, Hart DJ, Kandiah E, Boeri Erba E, Buisson A, Leonard G, Gutsch...
RgGuinier 3.9 nm
Dmax 11.7 nm
VolumePorod 217 nm3

SASDHY4 – Mitochondrial very long-chain specific acyl-CoA dehydrogenase enzyme, VLCAD

Very long-chain specific acyl-CoA dehydrogenase, mitochondrial experimental SAS data
DAMFILT model
Sample: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial dimer, 126 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Dec 2
Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angew Chem Int Ed Engl (2020)
Giachin G, Jessop M, Bouverot R, Acajjaoui S, Saidi M, Chretien A, Bacia-Verloop M, Signor L, Mas PJ, Favier A, Borel Meneroud E, Hons M, Hart DJ, Kandiah E, Boeri Erba E, Buisson A, Leonard G, Gutsch...
RgGuinier 3.4 nm
Dmax 9.9 nm
VolumePorod 215 nm3

SASDHZ4 – The C-terminal domain of ESCIT bound to a dimer of the complex I assembly factor ACAD9

Complex I assembly factor ACAD9, mitochondrialEvolutionarily conserved signaling intermediate in Toll pathway, mitochondrial experimental SAS data
GASBOR model
Sample: Complex I assembly factor ACAD9, mitochondrial dimer, 132 kDa Homo sapiens protein
Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial tetramer, 88 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Oct 4
Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angew Chem Int Ed Engl (2020)
Giachin G, Jessop M, Bouverot R, Acajjaoui S, Saidi M, Chretien A, Bacia-Verloop M, Signor L, Mas PJ, Favier A, Borel Meneroud E, Hons M, Hart DJ, Kandiah E, Boeri Erba E, Buisson A, Leonard G, Gutsch...
RgGuinier 6.0 nm
Dmax 16.5 nm
VolumePorod 683 nm3

SASDV46 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD

Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
...Giachin G, Assfalg M
RgGuinier 3.5 nm
Dmax 12.2 nm
VolumePorod 33 nm3

SASDV56 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317

Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-B experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317 Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
...Giachin G, Assfalg M
RgGuinier 3.3 nm
Dmax 13.3 nm
VolumePorod 41 nm3

SASDV66 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C353

Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-B experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C353 Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
...Giachin G, Assfalg M
RgGuinier 3.1 nm
Dmax 12.1 nm
VolumePorod 33 nm3

SASDV76 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to two Ubiquitins at tau residues C311 and C317

Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-BPolyubiquitin-B experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to two Ubiquitins at tau residues C311 and C317 Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
...Giachin G, Assfalg M
RgGuinier 3.3 nm
Dmax 12.2 nm
VolumePorod 59 nm3

SASDNF7 – CK2α (Casein kinase II subunit alpha)

Casein kinase II subunit alpha experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Casein kinase II subunit alpha monomer, 39 kDa Homo sapiens protein
Buffer: 25 mM Tris, 500 mM NaCl, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2021 Oct 10
Mechanism of CK2 Inhibition by a Ruthenium-Based Polyoxometalate. Front Mol Biosci 9:906390 (2022)
...Giachin G, Bellanda M, Borgo C, Ruzzene M, Spuri G, Campofelice A, Veneziano L, Bonchio M, Carraro M, Battistutta R
RgGuinier 2.2 nm
Dmax 6.7 nm
VolumePorod 59 nm3

SASDNG7 – CK2α (Casein kinase II subunit alpha) dimer bound to ruthenium-based polyoxometalate (Ru4POM)

Casein kinase II subunit alpha experimental SAS data
CUSTOM IN-HOUSE model
Sample: Casein kinase II subunit alpha dimer, 78 kDa Homo sapiens protein
Buffer: 25 mM Tris, 500 mM NaCl, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2021 Oct 10
Mechanism of CK2 Inhibition by a Ruthenium-Based Polyoxometalate. Front Mol Biosci 9:906390 (2022)
...Giachin G, Bellanda M, Borgo C, Ruzzene M, Spuri G, Campofelice A, Veneziano L, Bonchio M, Carraro M, Battistutta R
RgGuinier 3.0 nm
Dmax 11.8 nm
VolumePorod 122 nm3

SASDEW7 – C-terminal truncated bank vole prion protein (amino acids 90-231)

Major prion protein experimental SAS data
C-terminal truncated bank vole prion protein (amino acids 90-231) Rg histogram
Sample: Major prion protein monomer, 16 kDa Myodes glareolus protein
Buffer: 25 mM Ammonium Acetate, 250 mM NaCl, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Feb 25
Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain Biophysical Journal (2020)
...Giachin G
RgGuinier 2.3 nm
Dmax 9.4 nm
VolumePorod 29 nm3

SASDEX7 – C-terminal truncated bank vole prion protein (amino acids 90-231) bound to Cu(II)

Major prion protein experimental SAS data
C-terminal truncated bank vole prion protein (amino acids 90-231) bound to Cu(II) Rg histogram
Sample: Major prion protein monomer, 16 kDa Myodes glareolus protein
Buffer: 25 mM Ammonium Acetate, 250 mM NaCl, 0.001 mM CuSO4, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Feb 25
Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain Biophysical Journal (2020)
...Giachin G
RgGuinier 2.2 nm
Dmax 8.7 nm
VolumePorod 30 nm3

SASDEY7 – C-terminal truncated ovine prion protein ARR (amino acids 94-234)

Major prion protein experimental SAS data
C-terminal truncated ovine prion protein ARR (amino acids 94-234) Rg histogram
Sample: Major prion protein monomer, 16 kDa Ovis aries protein
Buffer: 25 mM Ammonium Acetate, 250 mM NaCl, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 4
Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain Biophysical Journal (2020)
...Giachin G
RgGuinier 2.2 nm
Dmax 9.0 nm
VolumePorod 29 nm3

SASDEZ7 – C-terminal truncated ovine prion protein (94-234) with ARR polymorphism + Cu(II)

Major prion protein experimental SAS data
C-terminal truncated ovine prion protein (94-234) with ARR polymorphism + Cu(II) Rg histogram
Sample: Major prion protein monomer, 16 kDa Ovis aries protein
Buffer: 25 mM Ammonium Acetate, 250 mM NaCl, 0.001 mM CuSO4, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 4
Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain Biophysical Journal (2020)
...Giachin G
RgGuinier 2.2 nm
Dmax 8.8 nm
VolumePorod 31 nm3

SASDE28 – C-terminal truncated ovine prion protein (94-234) with VRQ polymorphism

Major prion protein experimental SAS data
C-terminal truncated ovine prion protein (94-234) with VRQ polymorphism Rg histogram
Sample: Major prion protein monomer, 16 kDa Ovis aries protein
Buffer: 25 mM Ammonium Acetate, 250 mM NaCl, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 4
Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain Biophysical Journal (2020)
...Giachin G
RgGuinier 2.1 nm
Dmax 9.1 nm
VolumePorod 29 nm3

SASDE38 – C-terminal truncated ovine prion protein (94-234) with VRQ polymorphism + Cu(II)

Major prion protein experimental SAS data
C-terminal truncated ovine prion protein (94-234) with VRQ polymorphism + Cu(II) Rg histogram
Sample: Major prion protein monomer, 16 kDa Ovis aries protein
Buffer: 25 mM Ammonium Acetate, 250 mM NaCl, 0.001 mM CuSO4, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 4
Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain Biophysical Journal (2020)
...Giachin G
RgGuinier 2.2 nm
Dmax 8.7 nm
VolumePorod 29 nm3

SASDNB8 – Mature full length human prion protein

Major prion protein experimental SAS data
Mature full length human prion protein Rg histogram
Sample: Major prion protein monomer, 23 kDa Homo sapiens protein
Buffer: 10 mM HEPES 100 mM NaCl, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2020 Dec 13
A tetracationic porphyrin with dual anti-prion activity. iScience 26(9):107480 (2023)
...Giachin G, Tapella L, Comerio L, Restelli E, Raimondi I, Elezgarai SR, De Leo F, Quilici G, Taiarol L, Oldrati M, Lorenzo NL, García-Martínez S, Cagnotto A, Lucchetti J, Gobbi M, Vanni I, Nonno R, Di ...
RgGuinier 2.8 nm
Dmax 10.2 nm

SASDNC8 – Mature full length human prion protein in the presence of zinc-tetracationic porphyrin [Zn(II)-BnPyP]

Major prion protein experimental SAS data
Mature full length human prion protein in the presence of zinc-tetracationic porphyrin [Zn(II)-BnPyP] Rg histogram
Sample: Major prion protein monomer, 23 kDa Homo sapiens protein
Buffer: 10 mM HEPES 100 mM NaCl, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2020 Dec 13
A tetracationic porphyrin with dual anti-prion activity. iScience 26(9):107480 (2023)
...Giachin G, Tapella L, Comerio L, Restelli E, Raimondi I, Elezgarai SR, De Leo F, Quilici G, Taiarol L, Oldrati M, Lorenzo NL, García-Martínez S, Cagnotto A, Lucchetti J, Gobbi M, Vanni I, Nonno R, Di ...
RgGuinier 3.1 nm
Dmax 11.3 nm

SASDND8 – Mature full length human prion protein in the presence of a cationic Fe(III) porphyrin [Fe(III)-TMPyP]

Major prion protein experimental SAS data
Mature full length human prion protein in the presence of a cationic Fe(III) porphyrin [Fe(III)-TMPyP] Rg histogram
Sample: Major prion protein monomer, 23 kDa Homo sapiens protein
Buffer: 10 mM HEPES 100 mM NaCl, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2020 Dec 13
A tetracationic porphyrin with dual anti-prion activity. iScience 26(9):107480 (2023)
...Giachin G, Tapella L, Comerio L, Restelli E, Raimondi I, Elezgarai SR, De Leo F, Quilici G, Taiarol L, Oldrati M, Lorenzo NL, García-Martínez S, Cagnotto A, Lucchetti J, Gobbi M, Vanni I, Nonno R, Di ...
RgGuinier 2.8 nm
Dmax 10.3 nm

SASDSU8 – Threonine aldolase 1 tetramer at neutral pH

L-threonine aldolase experimental SAS data
PHENIX model
Sample: L-threonine aldolase tetramer, 165 kDa Mus musculus protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 1 mM DTT, pH: 7.8
Experiment: SAXS data collected at BM29, ESRF on 2023 Feb 14
One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse. Nat Commun 15(1):3199 (2024)
...Giachin G, Battistutta R, Contestabile R, Percudani R
RgGuinier 3.7 nm
Dmax 10.6 nm
VolumePorod 209 nm3

SASDRG9 – Stromal cell-derived factor 1, CXCL12

Stromal cell-derived factor 1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Stromal cell-derived factor 1 monomer, 9 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 11
The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12. Nat Commun 15(1):1201 (2024)
...Giachin G, Ghitti M, Bianchi ME, Musco G
RgGuinier 1.5 nm
Dmax 4.8 nm
VolumePorod 19 nm3

SASDRH9 – High mobility group protein B1, HMGB1

High mobility group protein B1 (D189E, E202D, E215D) experimental SAS data
High mobility group protein B1, HMGB1 Rg histogram
Sample: High mobility group protein B1 (D189E, E202D, E215D) monomer, 25 kDa Rattus norvegicus protein
Buffer: 20 mM Tris, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 11
The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12. Nat Commun 15(1):1201 (2024)
...Giachin G, Ghitti M, Bianchi ME, Musco G
RgGuinier 2.6 nm
Dmax 8.5 nm
VolumePorod 53 nm3

SASDRJ9 – High mobility group protein B1/Stromal cell-derived factor 1 complex (HMGB1-CXCL12)

Stromal cell-derived factor 1High mobility group protein B1 (D189E, E202D, E215D) experimental SAS data
Stromal cell-derived factor 1 High mobility group protein B1 (D189E, E202D, E215D) Kratky plot
Sample: Stromal cell-derived factor 1 monomer, 9 kDa Homo sapiens protein
High mobility group protein B1 (D189E, E202D, E215D) monomer, 25 kDa Rattus norvegicus protein
Buffer: 20 mM Tris, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 11
The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12. Nat Commun 15(1):1201 (2024)
...Giachin G, Ghitti M, Bianchi ME, Musco G
RgGuinier 2.9 nm
Dmax 10.5 nm
VolumePorod 72 nm3

SASDVQ9 – Full-length mature human mitochondrial ATP synthase subunit O (Oligomycin Sensitivity Conferral Protein or Complex V subunit O)

ATP synthase subunit O, mitochondrial experimental SAS data
ALPHAFOLD model
Sample: ATP synthase subunit O, mitochondrial dimer, 42 kDa Homo sapiens protein
Buffer: 50 mM Na2HPO4, 300 mM NaCl, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2022 Mar 15
The OSCP Subunit of ATP Synthase is a Dimer in Solution: Strategy to Induce the Monomeric Protein as a New Tool for Drug Discovery. J Mol Biol 437(17):169267 (2025)
...Giachin G, Sosic A, Bellanda M
RgGuinier 3.7 nm
Dmax 12.0 nm
VolumePorod 78 nm3

SASDVR9 – C-terminal tail of human mitochondrial ATP synthase subunit O (137-213) (Oligomycin Sensitivity Conferral Protein or Complex V subunit O)

ATP synthase subunit O, mitochondrial C-terminal section experimental SAS data
ALPHAFOLD model
Sample: ATP synthase subunit O, mitochondrial C-terminal section trimer, 25 kDa Homo sapiens protein
Buffer: 50 mM Na2HPO4, 300 mM NaCl, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2022 Mar 15
The OSCP Subunit of ATP Synthase is a Dimer in Solution: Strategy to Induce the Monomeric Protein as a New Tool for Drug Discovery. J Mol Biol 437(17):169267 (2025)
...Giachin G, Sosic A, Bellanda M
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 32 nm3