Browse by ORGANISM: Homo sapiens (Human)

SASDFY3 – Semi-synthetic nucleosome core particle (NCP) in complex with lysine-specific demethylase (LSD2) and the dehydrogenase domain plus linker of cytokine-like nuclear factor (NPAC delta-205)

Lysyne-specific Demethylase LSD2NPAC linker+DH (delta-205)Histone H3Histone H4Histone H2aHistone H2b147bp 601 Widom sequence experimental SAS data
Lysyne-specific Demethylase LSD2 NPAC linker+DH (delta-205) Histone H3 Histone H4 Histone H2a Histone H2b 147bp 601 Widom sequence Kratky plot
Sample: Lysyne-specific Demethylase LSD2 monomer, 89 kDa Homo sapiens protein
NPAC linker+DH (delta-205) tetramer, 150 kDa Homo sapiens protein
Histone H3 dimer, 31 kDa Xenopus laevis protein
Histone H4 dimer, 22 kDa Xenopus laevis protein
Histone H2a dimer, 28 kDa Xenopus laevis protein
Histone H2b dimer, 27 kDa Xenopus laevis protein
147bp 601 Widom sequence monomer, 45 kDa synthetic construct DNA
Buffer: 15 mM HEPES, 200 mM NaCl, pH: 7.3
Experiment: SAXS data collected at BM29, ESRF on 2017 Dec 11
A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex. Cell Rep 27(2):387-399.e7 (2019)
Marabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A
RgGuinier 7.8 nm
Dmax 30.4 nm
VolumePorod 1100 nm3

SASDE36 – Human ATP-citrate synthase (ACLY) in HBS

ATP-citrate synthase experimental SAS data
MULTIFOXS model
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 6
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 6.0 nm
Dmax 17.5 nm
VolumePorod 738 nm3

SASDE46 – Human ATP-citrate synthers (ACLY) in HBS + Citrate

ATP-citrate synthase experimental SAS data
ATP-citrate synthase Kratky plot
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 6
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 6.1 nm
Dmax 17.5 nm
VolumePorod 747 nm3

SASDE56 – Human ATP-citrate synthase (ACLY) in HBS + Citrate + Coenzyme-A

ATP-citrate synthase experimental SAS data
SASREF CV model
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM CoA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 5
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 5.8 nm
Dmax 16.5 nm
VolumePorod 709 nm3

SASDFA3 – Human ATP-citrate synthase (ACLY) full length in HBS

ATP-citrate synthase experimental SAS data
ATP-citrate synthase Kratky plot
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 6.1 nm
Dmax 19.0 nm
VolumePorod 765 nm3

SASDFB3 – Human ATP-citrate synthers (ACLY) full length in HBS + Citrate

ATP-citrate synthase experimental SAS data
ATP-citrate synthase Kratky plot
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 6.2 nm
Dmax 19.0 nm
VolumePorod 787 nm3

SASDFC3 – Human ATP-citrate synthase (ACLY) full length in HBS + Citrate + Coenzyme-A

ATP-citrate synthase experimental SAS data
MULTIFOXS model
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM CoA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 5.9 nm
Dmax 17.0 nm
VolumePorod 775 nm3

SASDET6 – Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7)

Polyglutamine-binding protein 1 p.Lys192Serfs*7 experimental SAS data
Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Lys192Serfs*7 dimer, 47 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
Rahman SK, Okazawa H, Chen YW
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 114 nm3

SASDEU6 – Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41)

Polyglutamine-binding protein 1 p.Arg153Serfs*41 experimental SAS data
Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Arg153Serfs*41 dimer, 44 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
Rahman SK, Okazawa H, Chen YW
RgGuinier 3.6 nm
Dmax 13.0 nm
VolumePorod 100 nm3

SASDDQ5 – Human metaphase chromosomes in 17mM magnesium chloride

Metaphase chromosomes in 17 mM magnesium chloride experimental SAS data
Metaphase chromosomes in 17 mM magnesium chloride Kratky plot
Sample: Metaphase chromosomes in 17 mM magnesium chloride monomer, 0 kDa Homo sapiens
Buffer: 10 mM PIPES, 17 mM magnesium chloride, 20 mM sodium chloride, 120 mM potassium chloride, 40% glycerol, pH: 7.2
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2013 May 23
Frozen-hydrated chromatin from metaphase chromosomes has an interdigitated multilayer structure. EMBO J 38(7) (2019)
Chicano A, Crosas E, Otón J, Melero R, Engel BD, Daban JR