Browse by MODEL: Hybrid

SASDLE3 – Ubiquitin activating enzyme 5 with ubiquitin-fold modifier 1 (UBA5 9 mg/mL + UFM1 2.25 mg/mL)

Ubiquitin-like modifier-activating enzyme 5Ubiquitin fold modifer 1 experimental SAS data
SASREF model
Sample: Ubiquitin-like modifier-activating enzyme 5 dimer, 68 kDa Homo sapiens protein
Ubiquitin fold modifer 1 monomer, 9 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Oct 29
Structure and dynamics of UBA5-UFM1 complex formation showing new insights in the UBA5 activation mechanism Journal of Structural Biology :107796 (2021)
Fuchs S, Kikhney A, Schubert R, Kaiser C, Liebau E, Svergun D, Betzel C, Perbandt M
RgGuinier 3.2 nm
Dmax 14.5 nm
VolumePorod 111 nm3

SASDM82 – Ubiquitin-fold modifier 1

Ubiquitin fold modifer 1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ubiquitin fold modifer 1 monomer, 9 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jun 13
Structure and dynamics of UBA5-UFM1 complex formation showing new insights in the UBA5 activation mechanism Journal of Structural Biology :107796 (2021)
Fuchs S, Kikhney A, Schubert R, Kaiser C, Liebau E, Svergun D, Betzel C, Perbandt M
RgGuinier 1.5 nm
Dmax 5.1 nm
VolumePorod 16 nm3

SASDK74 – Streptococcus agalactiae transcription factor BusR - RCK_C domain

Transcriptional repressor BusR RCK_C domain experimental SAS data
OTHER model
Sample: Transcriptional repressor BusR RCK_C domain dimer, 22 kDa Streptococcus agalactiae serotype … protein
Buffer: 100 mM NaCl, 30mM Hepes, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 2
BusR senses bipartite DNA binding motifs by a unique molecular ruler architecture. Nucleic Acids Res (2021)
Bandera AM, Bartho J, Lammens K, Drexler DJ, Kleinschwärzer J, Hopfner KP, Witte G
RgGuinier 1.9 nm
Dmax 6.4 nm
VolumePorod 44 nm3

SASDK94 – Streptococcus agalactiae transcription factor BusR dsDNA complex

Transcriptional repressor BusRBusR Recognition sequence experimental SAS data
OTHER model
Sample: Transcriptional repressor BusR tetramer, 95 kDa Streptococcus agalactiae protein
BusR Recognition sequence monomer, 28 kDa synthetic construct DNA
Buffer: 20mM HEPES, pH6.5, 100mM NaCl, 3% glycerol (v/v), pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 2
BusR senses bipartite DNA binding motifs by a unique molecular ruler architecture. Nucleic Acids Res (2021)
Bandera AM, Bartho J, Lammens K, Drexler DJ, Kleinschwärzer J, Hopfner KP, Witte G
RgGuinier 4.3 nm
Dmax 14.2 nm
VolumePorod 210 nm3

SASDKF6 – C2AB construct of synaptotagmin-1 (SYT1) with E395-397A mutations at the linker

Synaptotagmin-1 experimental SAS data
CORAL model
Sample: Synaptotagmin-1 monomer, 33 kDa Arabidopsis thaliana protein
Buffer: 50 mM Tris, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jun 11
The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites Life Science Alliance 4(10):e202101152 (2021)
Benavente J, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-López N, Botella M, Sánchez-Barrena M, Albert A
RgGuinier 3.1 nm
Dmax 12.1 nm
VolumePorod 59 nm3

SASDKG6 – SMP2C2A construct of synaptotagmin-1 (SYT1)

Synaptotagmin-1 (SYT1-SMP2C2A) experimental SAS data
MULTIFOXS model
Sample: Synaptotagmin-1 (SYT1-SMP2C2A) monomer, 72 kDa Escherichia coli protein
Buffer: 20 mM Tris, 100 mM NaCl, 5% glycerol, 2 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jun 11
The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites Life Science Alliance 4(10):e202101152 (2021)
Benavente J, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-López N, Botella M, Sánchez-Barrena M, Albert A
RgGuinier 4.2 nm
Dmax 17.8 nm
VolumePorod 138 nm3

SASDKJ9 – C2AB construct of synaptotagmin-1 (SYT1)

Synaptotagmin-1 experimental SAS data
DAMFILT model
Sample: Synaptotagmin-1 monomer, 33 kDa Arabidopsis thaliana protein
Buffer: 50 mM Tris, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Feb 16
The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites Life Science Alliance 4(10):e202101152 (2021)
Benavente J, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-López N, Botella M, Sánchez-Barrena M, Albert A
RgGuinier 2.8 nm
Dmax 12.6 nm
VolumePorod 50 nm3

SASDKK9 – C2AB construct of synaptotagmin-1 (SYT1) in presence of Ca cations

Synaptotagmin-1 experimental SAS data
MULTIFOXS model
Sample: Synaptotagmin-1 monomer, 33 kDa Arabidopsis thaliana protein
Buffer: 50 mM Tris, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Feb 16
The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites Life Science Alliance 4(10):e202101152 (2021)
Benavente J, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-López N, Botella M, Sánchez-Barrena M, Albert A
RgGuinier 2.9 nm
Dmax 13.8 nm
VolumePorod 54 nm3

SASDJD2 – Human respiratory syncytial virus A (RSV) phosphoprotein oligomerization domain

Phosphoprotein experimental SAS data
MULTIFOXS model
Sample: Phosphoprotein tetramer, 18 kDa Respiratory syncytial virus protein
Buffer: 20 mM Na phosphate 100 mM NaCl, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Jun 21
A Structural and Dynamic Analysis of the Partially Disordered Polymerase-Binding Domain in RSV Phosphoprotein Biomolecules 11(8):1225 (2021)
Cardone C, Caseau C, Bardiaux B, Thureaux A, Galloux M, Bajorek M, Eléouët J, Litaudon M, Bontems F, Sizun C
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 33 nm3

SASDLQ2 – PfMDH L-lactate dehydrogenase, apo

L-lactate dehydrogenase experimental SAS data
PYMOL model
Sample: L-lactate dehydrogenase tetramer, 141 kDa Plasmodium falciparum protein
Buffer: 100 mM Na-phosphate buffer, 400 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Xenocs Xeuss 2.0 with MetalJet, Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University on 2019 Jul 3
A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity Communications Biology 4(1) (2021)
Reyes Romero A, Lunev S, Popowicz G, Calderone V, Gentili M, Sattler M, Plewka J, Taube M, Kozak M, Holak T, Dömling A, Groves M
RgGuinier 3.4 nm
Dmax 10.5 nm
VolumePorod 211 nm3