Browse by MACROMOLECULE type: protein

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

SASDE66 – C. limicola ATP-citrate lyase (ACL) in HBS

ATP-citrate lyase experimental SAS data
ATP-citrate lyase Kratky plot
Sample: ATP-citrate lyase tetramer, 429 kDa Chlorobium limicola 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 20.0 nm
VolumePorod 666 nm3

SASDE76 – C. limicola ATP-citrate lyase (ACL) in HBS + Citrate

ATP-citrate lyase experimental SAS data
ATP-citrate lyase Kratky plot
Sample: ATP-citrate lyase tetramer, 429 kDa Chlorobium limicola 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 6.0 nm
Dmax 20.0 nm
VolumePorod 672 nm3

SASDE86 – C. limicola ATP-citrate lyase (ACL) in HBS + Citrate + Coenzyme-A

ATP-citrate lyase experimental SAS data
ATP-citrate lyase Kratky plot
Sample: ATP-citrate lyase tetramer, 429 kDa Chlorobium limicola 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 5.7 nm
Dmax 17.5 nm
VolumePorod 791 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

SASDEN9 – HcpR transcriptional regulator of Porphyromonas gingivalis

Hcp Transcriptional regulator experimental SAS data
HcpR transcriptional regulator of Porphyromonas gingivalis Rg histogram
Sample: Hcp Transcriptional regulator dimer, 51 kDa Porphyromonas gingivalis protein
Buffer: 25 mM Tris 150 mM NaCl 1mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jan 24
Nitrosative stress sensing in Porphyromonas gingivalis: structure of and heme binding by the transcriptional regulator HcpR. Acta Crystallogr D Struct Biol 75(Pt 4):437-450 (2019)
Belvin BR, Musayev FN, Burgner J, Scarsdale JN, Escalante CR, Lewis JP
RgGuinier 2.9 nm
Dmax 10.5 nm
VolumePorod 76 nm3