Browse by MACROMOLECULE type: protein

SASDDP9 – C-terminal half of pseudorabies virus tegument protein UL37

Tegument protein UL37 experimental SAS data
DAMMIN model
Sample: Tegument protein UL37 monomer, 49 kDa Suid alphaherpesvirus 1 protein
Buffer: 100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 3
The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 293(41):15827-15839 (2018)
Koenigsberg AL, Heldwein EE
RgGuinier 4.2 nm
Dmax 14.0 nm
VolumePorod 71 nm3

SASDDQ9 – N-terminal half of herpes simplex virus type-1 inner tegument protein UL37

Inner tegument protein experimental SAS data
DAMFILT model
Sample: Inner tegument protein monomer, 62 kDa Human alphaherpesvirus 1 protein
Buffer: 100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 3
The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 293(41):15827-15839 (2018)
Koenigsberg AL, Heldwein EE
RgGuinier 3.3 nm
Dmax 10.4 nm
VolumePorod 91 nm3

SASDEL4 – Residues 478-884 of pseudorabies virus tegument protein UL37

Tegument protein UL37 experimental SAS data
DAMMIN model
Sample: Tegument protein UL37 monomer, 43 kDa Suid alphaherpesvirus 1 protein
Buffer: 100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 3
The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 293(41):15827-15839 (2018)
Koenigsberg AL, Heldwein EE
RgGuinier 3.9 nm
Dmax 12.5 nm

SASDCW8 – Human Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 4mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 46 nm3

SASDCX8 – Human Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 47 nm3

SASDCY8 – Human Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 8mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 7.5 nm
VolumePorod 46 nm3

SASDCZ8 – Human Rev7 dimer in complex with Rev3 peptide @ 12.2 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.8 nm

SASDC29 – Human Rev7 dimer in complex with Rev3 peptide @ 10.6 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
HADDOCK model
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm
Dmax 11.0 nm
VolumePorod 108 nm3

SASDC39 – Human Rev7 dimer in complex with Rev3 peptide @ 9.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
HADDOCK model
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.0 nm
Dmax 11.4 nm
VolumePorod 107 nm3

SASDC49 – Human Rev7 dimer in complex with Rev3 peptide @ 6.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.1 nm
Dmax 11.6 nm
VolumePorod 105 nm3