SASBDB entries for UniProt ID:

SASDHT4 – Phosphoprotein from Nipah virus

UniProt ID: Q9IK91 (1-709) Phosphoprotein
Phosphoprotein experimental SAS data
Phosphoprotein Kratky plot
Sample: Phosphoprotein tetramer, 317 kDa Nipah henipavirus protein
Buffer: 20 mM Tris-HCL, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 3
Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1. Biophys J (2020)
Jensen MR, Yabukarski F, Communie G, Condamine E, Mas C, Volchkova V, Tarbouriech N, Bourhis JM, Volchkov V, Blackledge M, Jamin M
RgGuinier 10.9 nm
Dmax 39.3 nm

SASDHU4 – ECSIT C-terminal domain

UniProt ID: Q9BQ95 (249-431) Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
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, Gutsche I, Soler-Lopez M
RgGuinier 3.7 nm
Dmax 11.9 nm
VolumePorod 117 nm3

SASDHV4 – Mitochondrial complex I assembly factor, NDUFAF1

UniProt ID: Q9Y375 (25-327) Complex I intermediate-associated protein 30, mitochondrial
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, Gutsche I, Soler-Lopez M
RgGuinier 3.3 nm
Dmax 9.6 nm
VolumePorod 82 nm3

SASDHW4 – Mitochondrial Complex I assembly factor, ACAD9

UniProt ID: Q9H845 (38-621) Complex I assembly factor ACAD9, mitochondrial
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, Gutsche I, Soler-Lopez M
RgGuinier 3.6 nm
Dmax 10.2 nm
VolumePorod 217 nm3

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

UniProt ID: P49748 (72-655) Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
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, Gutsche I, Soler-Lopez M
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

UniProt ID: Q9H845 (38-621) Complex I assembly factor ACAD9, mitochondrial

UniProt ID: Q9BQ95 (249-431) Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
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, Gutsche I, Soler-Lopez M
RgGuinier 6.0 nm
Dmax 16.5 nm
VolumePorod 683 nm3

SASDH25 – Actinobacterial phosphodiesterase targeting cyclic di-AMP (AtaC)

UniProt ID: F2R7Z6 (1-401) Alkaline phosphodiesterase I or Nucleotide pyrophosphatase
Alkaline phosphodiesterase I or Nucleotide pyrophosphatase experimental SAS data
Alkaline phosphodiesterase I or Nucleotide pyrophosphatase Kratky plot
Sample: Alkaline phosphodiesterase I or Nucleotide pyrophosphatase monomer, 46 kDa Streptomyces venezuelae protein
Buffer: 20 mM HEPES, 200mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 17
c-di-AMP hydrolysis by a novel type of phosphodiesterase promotes differentiation of multicellular bacteria (2019)
Latoscha A, Drexler D, Al-Bassam M, Kaever V, Findlay K, Witte G, Tschowri N
RgGuinier 2.4 nm
Dmax 7.8 nm
VolumePorod 74 nm3

SASDH35 – Soluble cyclic di-AMP binding protein CpeA (vnz_28055), regulator of CpeB

UniProt ID: F2R9B6 (6-161) Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein)
Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein) experimental SAS data
Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein) Kratky plot
Sample: Cyclic di-AMP binding protein (Putative regulatory, ligand-binding protein) dimer, 38 kDa Streptomyces venezuelae protein
Buffer: 200 mM NaCl, 30 mM NaPi, 5% (v/v) glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 4
c-di-AMP hydrolysis by a novel type of phosphodiesterase promotes differentiation of multicellular bacteria (2019)
Latoscha A, Drexler D, Al-Bassam M, Kaever V, Findlay K, Witte G, Tschowri N
RgGuinier 2.8 nm
Dmax 9.2 nm
VolumePorod 69 nm3

SASDH45 – Histone Deacetylase 1 (HDAC1) and Lysine-specific Demethylase 1 (LSD1) in the complex with CoREST

UniProt ID: Q13547 (1-482) Histone deacetylase 1

UniProt ID: O60341 (1-852) Lysine-specific histone demethylase 1A

UniProt ID: Q9UKL0 (86-485) REST corepressor 1
Histone deacetylase 1Lysine-specific histone demethylase 1AREST corepressor 1 experimental SAS data
DAMFILT model
Sample: Histone deacetylase 1 monomer, 55 kDa Homo sapiens protein
Lysine-specific histone demethylase 1A monomer, 93 kDa Homo sapiens protein
REST corepressor 1 monomer, 46 kDa Homo sapiens protein
Buffer: 25 mM Tris/Cl, 50 mM potassium acetate and 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2015 Jan 23
Mechanism of Crosstalk between the LSD1 Demethylase and HDAC1 Deacetylase in the CoREST Complex. Cell Rep 30(8):2699-2711.e8 (2020)
Song Y, Dagil L, Fairall L, Robertson N, Wu M, Ragan TJ, Savva CG, Saleh A, Morone N, Kunze MBA, Jamieson AG, Cole PA, Hansen DF, Schwabe JWR
RgGuinier 6.0 nm
Dmax 15.8 nm
VolumePorod 437 nm3

SASDH65 – Poly(rC)-binding protein 2 (PCBP2)

UniProt ID: Q15366 (1-365) Poly(rC)-binding protein 2
Poly(rC)-binding protein 2 experimental SAS data
Poly(rC)-binding protein 2 Kratky plot
Sample: Poly(rC)-binding protein 2 monomer, 40 kDa Homo sapiens protein
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Jul 16
Structure of the PCBP2/stem-loop IV complex underlying translation initiation mediated by the poliovirus type I IRES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 3.3 nm
Dmax 13.2 nm
VolumePorod 76 nm3