Browse by MODEL: Hybrid

SASDFR4 – HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli (Domain A (PDB:3MLI)-Linker (PDB:1BR0)-Domain B (PDB:1WRT))

HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli experimental SAS data
CORAL model
Sample: HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli tetramer, 150 kDa Helicobacter pylori, Rattus … protein
Buffer: 20 mM Tris-HCl 150 mM NaCl, pH: 8
Experiment: SAXS data collected at Rigaku Nano-Viewer, Nara Institute of Science and Technology on 2016 Dec 8
Construction of a Quadrangular Tetramer and a Cage-Like Hexamer from Three-Helix Bundle-Linked Fusion Proteins. ACS Synth Biol (2019)
Miyamoto T, Hayashi Y, Yoshida K, Watanabe H, Uchihashi T, Yonezawa K, Shimizu N, Kamikubo H, Hirota S
RgGuinier 5.1 nm
Dmax 20.0 nm
VolumePorod 379 nm3

SASDFS4 – HP0242 from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, de novo designed coiled-coil trimer domain (Domain A (PDB:3MLI)-Linker (PDB:1BR0)-Domain B (PDB:4DZL))

HP0242 from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, de novo designed coiled-coil trimer domain experimental SAS data
CORAL model
Sample: HP0242 from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, de novo designed coiled-coil trimer domain hexamer, 179 kDa Helicobacter pylori, Rattus … protein
Buffer: 20 mM Tris-HCl 150 mM NaCl, pH: 8
Experiment: SAXS data collected at Rigaku Nano-Viewer, Nara Institute of Science and Technology on 2017 Mar 29
Construction of a Quadrangular Tetramer and a Cage-Like Hexamer from Three-Helix Bundle-Linked Fusion Proteins. ACS Synth Biol (2019)
Miyamoto T, Hayashi Y, Yoshida K, Watanabe H, Uchihashi T, Yonezawa K, Shimizu N, Kamikubo H, Hirota S
RgGuinier 6.5 nm
Dmax 24.0 nm
VolumePorod 642 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

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

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

SASDKN2 – Matrix protein from Newcastle disease virus at neutral pH

Matrix protein experimental SAS data
DAMMIN model
Sample: Matrix protein, 40 kDa Newcastle disease virus … protein
Buffer: STE buffer 100 mM NaCl, 10 mM Tris-HCl, and 1 mM EDTA, pH: 4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 11
Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH Journal of Virology 93(6) (2019)
Shtykova E, Petoukhov M, Dadinova L, Fedorova N, Tashkin V, Timofeeva T, Ksenofontov A, Loshkarev N, Baratova L, Jeffries C, Svergun D, Batishchev O, García-Sastre A
RgGuinier 3.5 nm

SASDKP2 – Matrix protein from Newcastle disease virus at acidic pH

Matrix protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Matrix protein dimer, 79 kDa Newcastle disease virus … protein
Buffer: STE buffer 100 mM NaCl, 10 mM Tris-HCl, and 1 mM EDTA, pH: 4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 11
Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH Journal of Virology 93(6) (2019)
Shtykova E, Petoukhov M, Dadinova L, Fedorova N, Tashkin V, Timofeeva T, Ksenofontov A, Loshkarev N, Baratova L, Jeffries C, Svergun D, Batishchev O, García-Sastre A
RgGuinier 3.3 nm

SASDC28 – Mature α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) trimer, 81 kDa Wolbachia endosymbiont of … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2014 Mar 29
The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
Walden PM, Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL
RgGuinier 2.8 nm
Dmax 8.7 nm
VolumePorod 913 nm3

SASDC38 – Truncated α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) monomer, 21 kDa Wolbachia endosymbiont of … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29
The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
Walden PM, Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL
RgGuinier 1.9 nm
Dmax 6.3 nm
VolumePorod 275 nm3

SASDEK4 – C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (ScsC)

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein experimental SAS data
DAMFILT model
Sample: C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis. Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019)
Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL
RgGuinier 1.7 nm
Dmax 5.4 nm
VolumePorod 22200 nm3