SASBDB entries for UniProt ID:

SASDL75 – Maltose Binding Protein (MBP) fused to Drosophila Melanogaster SMN186–220: Tetramer analyzed by SVD-EFA SEC-SAXS

UniProt ID: Q9VV74 (186-220) Survival motor neuron protein

UniProt ID: P0AEX9 (1-396) Maltose/maltodextrin-binding periplasmic protein
Survival motor neuron proteinMaltose/maltodextrin-binding periplasmic protein experimental SAS data
Survival motor neuron protein Maltose/maltodextrin-binding periplasmic protein Kratky plot
Sample: Survival motor neuron protein tetramer, 15 kDa Drosophila melanogaster protein
Maltose/maltodextrin-binding periplasmic protein tetramer, 174 kDa Escherichia coli (strain … protein
Buffer: 20 mM Na/KPO4 pH 7.0, 300 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 19
Assembly of higher-order SMN oligomers is essential for metazoan viability and requires an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 3.9 nm
Dmax 11.3 nm
VolumePorod 340 nm3

SASDL85 – Maltose Binding Protein (MBP) fused to Drosophila Melanogaster SMN186–220: Octamer analyzed by SVD-EFA SEC-SAXS

UniProt ID: P0AEX9 (1-396) Maltose/maltodextrin-binding periplasmic protein

UniProt ID: Q9VV74 (186-220) Survival motor neuron protein
Maltose/maltodextrin-binding periplasmic proteinSurvival motor neuron protein experimental SAS data
Maltose/maltodextrin-binding periplasmic protein Survival motor neuron protein Kratky plot
Sample: Maltose/maltodextrin-binding periplasmic protein octamer, 347 kDa Escherichia coli (strain … protein
Survival motor neuron protein octamer, 31 kDa Drosophila melanogaster protein
Buffer: 20 mM Na/KPO4 pH 7.0, 300 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 19
Assembly of higher-order SMN oligomers is essential for metazoan viability and requires an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 5.6 nm
Dmax 17.9 nm
VolumePorod 800 nm3

SASDL95 – Drosophila Melanogaster Gemin2-SMN: Octamer analyzed by SVD-EFA SEC-SAXS

UniProt ID: Q9VVX0 (1-245) Protein Gemin2

UniProt ID: Q9VV74 (1-226) Survival motor neuron protein
Protein Gemin2Survival motor neuron protein experimental SAS data
Protein Gemin2 Survival motor neuron protein Kratky plot
Sample: Protein Gemin2 octamer, 230 kDa Drosophila melanogaster protein
Survival motor neuron protein octamer, 197 kDa Drosophila melanogaster protein
Buffer: 20 mM Na/KPO4 pH 7.0, 300 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 19
Assembly of higher-order SMN oligomers is essential for metazoan viability and requires an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 7.8 nm
Dmax 28.7 nm
VolumePorod 2660 nm3

SASDLA5 – Wild-type human myelin protein P2

UniProt ID: P02689 (1-132) Myelin P2 protein
Myelin P2 protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin P2 protein monomer, 15 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jul 22
Human myelin protein P2: from crystallography to time-lapse membrane imaging and neuropathy-associated variants. FEBS J (2021)
Uusitalo M, Klenow MB, Laulumaa S, Blakeley MP, Simonsen AC, Ruskamo S, Kursula P
RgGuinier 1.5 nm
Dmax 4.2 nm
VolumePorod 17 nm3

SASDLE5 – RORg2 bound to a Classic-RORgamma Response Element

UniProt ID: P51449 (25-518) Retinoid-related orphan receptor-gamma

UniProt ID: None (None-None) Classic-RORgamma Response Element
Retinoid-related orphan receptor-gammaClassic-RORgamma Response Element experimental SAS data
RORg2 bound to a Classic-RORgamma Response Element Rg histogram
Sample: Retinoid-related orphan receptor-gamma monomer, 56 kDa Homo sapiens protein
Classic-RORgamma Response Element dimer, 19 kDa Homo sapiens DNA
Buffer: 25 mM HEPES, 150 mM TCEP, 2% Glycerol, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Nov 20
Conformational Changes of RORγ During Response Element Recognition and Coregulator Engagement Journal of Molecular Biology :167258 (2021)
Strutzenberg T, Zhu Y, Novick S, Garcia-Ordonez R, Doebelin C, He Y, Ra Chang M, Kamenecka T, Edwards D, Griffin P
RgGuinier 5.5 nm
Dmax 22.9 nm
VolumePorod 132 nm3

SASDLF5 – RORg2 bound to a Variant-RORgamma Response Element

UniProt ID: P51449 (25-518) Retinoid-related orphan receptor-gamma

UniProt ID: None (None-None) Variant-RORgamma Response Element
Retinoid-related orphan receptor-gammaVariant-RORgamma Response Element experimental SAS data
RORg2 bound to a Variant-RORgamma Response Element Rg histogram
Sample: Retinoid-related orphan receptor-gamma monomer, 56 kDa Homo sapiens protein
Variant-RORgamma Response Element dimer, 18 kDa Homo sapiens DNA
Buffer: 25 mM HEPES, 150 mM TCEP, 2% Glycerol, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Nov 20
Conformational Changes of RORγ During Response Element Recognition and Coregulator Engagement Journal of Molecular Biology :167258 (2021)
Strutzenberg T, Zhu Y, Novick S, Garcia-Ordonez R, Doebelin C, He Y, Ra Chang M, Kamenecka T, Edwards D, Griffin P
RgGuinier 4.4 nm
Dmax 22.1 nm
VolumePorod 112 nm3

SASDLG5 – Human nerve growth factor

UniProt ID: P01138 (131-239) Beta-nerve growth factor
Beta-nerve growth factor experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-nerve growth factor dimer, 24 kDa Homo sapiens protein
Buffer: 50 mM Na-phosphate, 1 mM EDTA, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jul 2
The conundrum of the high-affinity NGF binding site formation unveiled? Biophys J 108(3):687-97 (2015)
Covaceuszach S, Konarev PV, Cassetta A, Paoletti F, Svergun DI, Lamba D, Cattaneo A
RgGuinier 2.5 nm

SASDLH5 – Aggregation state of Ataxin-3 protein

UniProt ID: P54252 (1-361) Ataxin-3
Ataxin-3 experimental SAS data
DAMMIN model
Sample: Ataxin-3 monomer, 41 kDa Homo sapiens protein
Buffer: phosphate buffered saline (PBS), pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Dec 3
Interactions of ataxin-3 with its molecular partners in the protein machinery that sorts protein aggregates to the aggresome. Int J Biochem Cell Biol 51:58-64 (2014)
Bonanomi M, Mazzucchelli S, D'Urzo A, Nardini M, Konarev PV, Invernizzi G, Svergun DI, Vanoni M, Regonesi ME, Tortora P
RgGuinier 6.9 nm
Dmax 25.0 nm
VolumePorod 425 nm3

SASDLJ5 – Aggregation state of tubulin protein

UniProt ID: Q71U36 (1-451) Tubulin alpha-1A chain
Tubulin alpha-1A chain experimental SAS data
DAMMIN model
Sample: Tubulin alpha-1A chain monomer, 50 kDa Homo sapiens protein
Buffer: phosphate buffered saline (PBS), pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Dec 3
Interactions of ataxin-3 with its molecular partners in the protein machinery that sorts protein aggregates to the aggresome. Int J Biochem Cell Biol 51:58-64 (2014)
Bonanomi M, Mazzucchelli S, D'Urzo A, Nardini M, Konarev PV, Invernizzi G, Svergun DI, Vanoni M, Regonesi ME, Tortora P
RgGuinier 7.0 nm
Dmax 25.0 nm
VolumePorod 340 nm3

SASDLK5 – Aggregation state of ataxin-3-tubulin complex

UniProt ID: P54252 (1-361) Ataxin-3

UniProt ID: Q71U36 (1-451) Tubulin alpha-1A chain
Ataxin-3Tubulin alpha-1A chain experimental SAS data
DAMMIN model
Sample: Ataxin-3 monomer, 41 kDa Homo sapiens protein
Tubulin alpha-1A chain monomer, 50 kDa Homo sapiens protein
Buffer: phosphate buffered saline (PBS), pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Dec 3
Interactions of ataxin-3 with its molecular partners in the protein machinery that sorts protein aggregates to the aggresome. Int J Biochem Cell Biol 51:58-64 (2014)
Bonanomi M, Mazzucchelli S, D'Urzo A, Nardini M, Konarev PV, Invernizzi G, Svergun DI, Vanoni M, Regonesi ME, Tortora P
RgGuinier 8.4 nm
Dmax 30.0 nm
VolumePorod 900 nm3