SASBDB entries for UniProt ID:

SASDRU8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 300 mM NaCl

UniProt ID: P06450 (1-507) ATP synthase subunit alpha, chloroplastic

UniProt ID: P00825 (1-498) ATP synthase subunit beta, chloroplastic

UniProt ID: P05435 (1-364) ATP synthase gamma chain, chloroplastic

UniProt ID: P11402 (1-257) ATP synthase delta chain, chloroplastic

UniProt ID: P00833 (1-134) ATP synthase epsilon chain, chloroplastic

UniProt ID: P06451 (1-247) ATP synthase subunit a, chloroplastic

UniProt ID: P06453 (1-184) ATP synthase subunit b, chloroplastic

UniProt ID: P31853 (1-222) ATP synthase subunit b', chloroplastic

UniProt ID: P69447 (1-81) ATP synthase subunit c, chloroplastic

UniProt ID: None (None-None) 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside
ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
OTHER [STATIC IMAGE] model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 300 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
Osipov S, Ryzhykau Y, Zinovev E, Minaeva A, Ivashchenko S, Verteletskiy D, Sudarev V, Kuklina D, Nikolaev M, Semenov Y, Zagryadskaya Y, Okhrimenko I, Gette M, Dronova E, Shishkin A, Dencher N, Kuklin A, Ivanovich V, Uversky V, Vlasov A
RgGuinier 7.8 nm
Dmax 39.5 nm
VolumePorod 1127 nm3

SASDRV8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 350 mM NaCl

UniProt ID: P06450 (1-507) ATP synthase subunit alpha, chloroplastic

UniProt ID: P00825 (1-498) ATP synthase subunit beta, chloroplastic

UniProt ID: P05435 (1-364) ATP synthase gamma chain, chloroplastic

UniProt ID: P11402 (1-257) ATP synthase delta chain, chloroplastic

UniProt ID: P00833 (1-134) ATP synthase epsilon chain, chloroplastic

UniProt ID: P06451 (1-247) ATP synthase subunit a, chloroplastic

UniProt ID: P06453 (1-184) ATP synthase subunit b, chloroplastic

UniProt ID: P31853 (1-222) ATP synthase subunit b', chloroplastic

UniProt ID: P69447 (1-81) ATP synthase subunit c, chloroplastic

UniProt ID: None (None-None) 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside
ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
OTHER [STATIC IMAGE] model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 350 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
Osipov S, Ryzhykau Y, Zinovev E, Minaeva A, Ivashchenko S, Verteletskiy D, Sudarev V, Kuklina D, Nikolaev M, Semenov Y, Zagryadskaya Y, Okhrimenko I, Gette M, Dronova E, Shishkin A, Dencher N, Kuklin A, Ivanovich V, Uversky V, Vlasov A
RgGuinier 8.9 nm
Dmax 44.5 nm
VolumePorod 1150 nm3

SASDRW8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 450 mM NaCl

UniProt ID: P06450 (1-507) ATP synthase subunit alpha, chloroplastic

UniProt ID: P00825 (1-498) ATP synthase subunit beta, chloroplastic

UniProt ID: P05435 (1-364) ATP synthase gamma chain, chloroplastic

UniProt ID: P11402 (1-257) ATP synthase delta chain, chloroplastic

UniProt ID: P00833 (1-134) ATP synthase epsilon chain, chloroplastic

UniProt ID: P06451 (1-247) ATP synthase subunit a, chloroplastic

UniProt ID: P06453 (1-184) ATP synthase subunit b, chloroplastic

UniProt ID: P31853 (1-222) ATP synthase subunit b', chloroplastic

UniProt ID: P69447 (1-81) ATP synthase subunit c, chloroplastic

UniProt ID: None (None-None) 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside
ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
OTHER [STATIC IMAGE] model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 450 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
Osipov S, Ryzhykau Y, Zinovev E, Minaeva A, Ivashchenko S, Verteletskiy D, Sudarev V, Kuklina D, Nikolaev M, Semenov Y, Zagryadskaya Y, Okhrimenko I, Gette M, Dronova E, Shishkin A, Dencher N, Kuklin A, Ivanovich V, Uversky V, Vlasov A
RgGuinier 10.8 nm
Dmax 46.5 nm
VolumePorod 1703 nm3

SASDR39 – MBP-, SUMO-fused heterodimeric SEPT6-SEPT7 septin coiled coil (MBP-SEPT6c+SUMO-SEPT7c)

UniProt ID: Q14141 (317-427) Septin-6 (C-terminal domain of SEPT6 fused to his-tagged MBP)

UniProt ID: Q16181 (335-437) Septin-7 (C-terminal domain of SEPT7 fused to SUMO)
Septin-6 (C-terminal domain of SEPT6 fused to his-tagged MBP)Septin-7 (C-terminal domain of SEPT7 fused to SUMO) experimental SAS data
MULTIFOXS model
Sample: Septin-6 (C-terminal domain of SEPT6 fused to his-tagged MBP) monomer, 55 kDa Homo sapiens protein
Septin-7 (C-terminal domain of SEPT7 fused to SUMO) monomer, 25 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Feb 3
X-ray structure of the metastable SEPT14-SEPT7 coiled coil reveals a hendecad region crucial for heterodimerization. Acta Crystallogr D Struct Biol (2023)
Cavini IA, Winter AJ, D'Muniz Pereira H, Woolfson DN, Crump MP, Garratt RC
RgGuinier 5.4 nm
Dmax 21.5 nm
VolumePorod 142 nm3

SASDR49 – MBP-, SUMO-fused heterodimeric SEPT8-SEPT7 septin coiled coil (MBP-SEPT8c+SUMO-SEPT7c)

UniProt ID: Q16181 (335-437) Septin-7 (C-terminal domain of SEPT7 fused to SUMO)

UniProt ID: Q92599 (319-429) Septin-8 (C-terminal domain of SEPT8 fused to MBP)
Septin-7 (C-terminal domain of SEPT7 fused to SUMO)Septin-8 (C-terminal domain of SEPT8 fused to MBP) experimental SAS data
MULTIFOXS model
Sample: Septin-7 (C-terminal domain of SEPT7 fused to SUMO) monomer, 25 kDa Homo sapiens protein
Septin-8 (C-terminal domain of SEPT8 fused to MBP) monomer, 55 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Feb 3
X-ray structure of the metastable SEPT14-SEPT7 coiled coil reveals a hendecad region crucial for heterodimerization. Acta Crystallogr D Struct Biol (2023)
Cavini IA, Winter AJ, D'Muniz Pereira H, Woolfson DN, Crump MP, Garratt RC
RgGuinier 5.3 nm
Dmax 19.9 nm
VolumePorod 140 nm3

SASDR59 – MBP-, SUMO-fused heterodimeric SEPT10-SEPT7 septin coiled coil (MBP-SEPT10c+SUMO-SEPT7c)

UniProt ID: Q16181 (335-437) Septin-7 (C-terminal domain of SEPT7 fused to SUMO)

UniProt ID: Q9P0V9 (341-454) Septin-10 (C-terminal domain of SEPT10 fused to MBP)
Septin-7 (C-terminal domain of SEPT7 fused to SUMO)Septin-10 (C-terminal domain of SEPT10 fused to MBP) experimental SAS data
DAMMIN model
Sample: Septin-7 (C-terminal domain of SEPT7 fused to SUMO) monomer, 25 kDa Homo sapiens protein
Septin-10 (C-terminal domain of SEPT10 fused to MBP) monomer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Feb 3
X-ray structure of the metastable SEPT14-SEPT7 coiled coil reveals a hendecad region crucial for heterodimerization. Acta Crystallogr D Struct Biol (2023)
Cavini IA, Winter AJ, D'Muniz Pereira H, Woolfson DN, Crump MP, Garratt RC
RgGuinier 5.7 nm
Dmax 21.7 nm
VolumePorod 154 nm3

SASDR69 – MBP-, SUMO-fused heterodimeric SEPT11-SEPT7 septin coiled coil (MBP-SEPT11c+SUMO-SEPT7c)

UniProt ID: Q16181 (335-437) Septin-7 (C-terminal domain of SEPT7 fused to SUMO)

UniProt ID: Q9NVA2 (316-429) Septin-11 (C-terminal domain of SEPT11 fused to MBP)
Septin-7 (C-terminal domain of SEPT7 fused to SUMO)Septin-11 (C-terminal domain of SEPT11 fused to MBP) experimental SAS data
MULTIFOXS model
Sample: Septin-7 (C-terminal domain of SEPT7 fused to SUMO) monomer, 25 kDa Homo sapiens protein
Septin-11 (C-terminal domain of SEPT11 fused to MBP) monomer, 55 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Feb 3
X-ray structure of the metastable SEPT14-SEPT7 coiled coil reveals a hendecad region crucial for heterodimerization. Acta Crystallogr D Struct Biol (2023)
Cavini IA, Winter AJ, D'Muniz Pereira H, Woolfson DN, Crump MP, Garratt RC
RgGuinier 5.2 nm
Dmax 20.9 nm
VolumePorod 139 nm3

SASDR79 – MBP-, SUMO-fused heterodimeric SEPT14-SEPT7 septin coiled coil (MBP-SEPT14c+SUMO-SEPT7c)

UniProt ID: Q16181 (335-437) Septin-7 (C-terminal domain of SEPT7 fused to SUMO)

UniProt ID: Q6ZU15 (327-432) Septin-14 (C-terminal domain of SEPT14 fused to MBP)
Septin-7 (C-terminal domain of SEPT7 fused to SUMO)Septin-14 (C-terminal domain of SEPT14 fused to MBP) experimental SAS data
MULTIFOXS model
Sample: Septin-7 (C-terminal domain of SEPT7 fused to SUMO) monomer, 25 kDa Homo sapiens protein
Septin-14 (C-terminal domain of SEPT14 fused to MBP) monomer, 55 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Feb 3
X-ray structure of the metastable SEPT14-SEPT7 coiled coil reveals a hendecad region crucial for heterodimerization. Acta Crystallogr D Struct Biol (2023)
Cavini IA, Winter AJ, D'Muniz Pereira H, Woolfson DN, Crump MP, Garratt RC
RgGuinier 5.1 nm
Dmax 20.3 nm
VolumePorod 143 nm3

SASDR89 – Aromatic-L-amino-acid decarboxylase (AADC) - apo form

UniProt ID: P20711 (None-None) Aromatic-L-amino-acid decarboxylase (M17V)
Aromatic-L-amino-acid decarboxylase (M17V) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (M17V) dimer, 108 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 28
Human aromatic amino acid decarboxylase is an asymmetric and flexible enzyme: implication in AADC deficiency Protein Science (2023)
Bisello G, Ribeiro R, Perduca M, Belviso B, Polverino de' Laureto P, Giorgetti A, Caliandro R, Bertoldi M
RgGuinier 3.4 nm
Dmax 15.8 nm
VolumePorod 181 nm3

SASDR99 – Aromatic-L-amino-acid decarboxylase (AADC) - pyridoxal 5'-phosphate bound holo form

UniProt ID: P20711 (None-None) Aromatic-L-amino-acid decarboxylase (M17V)
Aromatic-L-amino-acid decarboxylase (M17V) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (M17V) dimer, 108 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 28
Human aromatic amino acid decarboxylase is an asymmetric and flexible enzyme: implication in AADC deficiency Protein Science (2023)
Bisello G, Ribeiro R, Perduca M, Belviso B, Polverino de' Laureto P, Giorgetti A, Caliandro R, Bertoldi M
RgGuinier 3.2 nm
Dmax 14.9 nm
VolumePorod 180 nm3