Browse by MODEL: Hybrid

SASDGK5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH) (Paused SEC)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 7.2 nm
VolumePorod 30 nm3

SASDFC4 – Condensin complex subunit 3-like protein, Ycg1, extrapolated to infinite dilution

Condensin complex subunit 3-like protein experimental SAS data
DAMMIF model
Sample: Condensin complex subunit 3-like protein monomer, 108 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 20
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1. J Biol Chem 294(37):13822-13829 (2019)
Manalastas-Cantos K, Kschonsak M, Haering CH, Svergun DI
RgGuinier 4.6 nm
Dmax 15.6 nm
VolumePorod 236 nm3

SASDFD4 – Condensin complex subunit 3-like protein,Ycg1, bound to condensin complex subunit 2, Brn1 (Ycg1-Brn1)

Condensin complex subunit 3-like proteinCondensin complex subunit 2 experimental SAS data
DAMMIF model
Sample: Condensin complex subunit 3-like protein monomer, 108 kDa Chaetomium thermophilum protein
Condensin complex subunit 2 monomer, 17 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 20
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1. J Biol Chem 294(37):13822-13829 (2019)
Manalastas-Cantos K, Kschonsak M, Haering CH, Svergun DI
RgGuinier 4.3 nm
Dmax 13.7 nm
VolumePorod 230 nm3

SASDFE4 – Condensin complex subunit 3-like protein, Ycg1, at 10mg/ml (tetramer)

Condensin complex subunit 3-like protein experimental SAS data
SASREF MX model
Sample: Condensin complex subunit 3-like protein tetramer, 433 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 20
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1. J Biol Chem 294(37):13822-13829 (2019)
Manalastas-Cantos K, Kschonsak M, Haering CH, Svergun DI
RgGuinier 8.3 nm
Dmax 32.7 nm
VolumePorod 1080 nm3

SASDFF4 – Condensin complex subunit 3-like protein, Ycg1, at 5mg/ml

Condensin complex subunit 3-like proteinCondensin complex subunit 3-like protein experimental SAS data
SASREF MX model
Sample: Condensin complex subunit 3-like protein tetramer, 433 kDa Chaetomium thermophilum protein
Condensin complex subunit 3-like protein dimer, 217 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 20
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1. J Biol Chem 294(37):13822-13829 (2019)
Manalastas-Cantos K, Kschonsak M, Haering CH, Svergun DI
RgGuinier 6.8 nm
Dmax 29.8 nm
VolumePorod 720 nm3

SASDFG4 – Condensin complex subunit 3-like protein, Ycg1, at 2mg/ml (dimer)

Condensin complex subunit 3-like protein experimental SAS data
SASREF MX model
Sample: Condensin complex subunit 3-like protein dimer, 217 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 20
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1. J Biol Chem 294(37):13822-13829 (2019)
Manalastas-Cantos K, Kschonsak M, Haering CH, Svergun DI
RgGuinier 5.4 nm
Dmax 19.0 nm
VolumePorod 463 nm3

SASDFH4 – Condensin complex subunit 3-like protein, Ycg1, at 1mg/ml

Condensin complex subunit 3-like proteinCondensin complex subunit 3-like protein experimental SAS data
SASREF MX model
Sample: Condensin complex subunit 3-like protein monomer, 108 kDa Chaetomium thermophilum protein
Condensin complex subunit 3-like protein dimer, 217 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 20
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1. J Biol Chem 294(37):13822-13829 (2019)
Manalastas-Cantos K, Kschonsak M, Haering CH, Svergun DI
RgGuinier 5.3 nm
Dmax 18.7 nm
VolumePorod 400 nm3

SASDFJ4 – Condensin complex subunit 3-like protein, Ycg1, at 0.5mg/ml

Condensin complex subunit 3-like proteinCondensin complex subunit 3-like protein experimental SAS data
SASREF MX model
Sample: Condensin complex subunit 3-like protein monomer, 108 kDa Chaetomium thermophilum protein
Condensin complex subunit 3-like protein dimer, 217 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 20
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1. J Biol Chem 294(37):13822-13829 (2019)
Manalastas-Cantos K, Kschonsak M, Haering CH, Svergun DI
RgGuinier 4.7 nm
Dmax 16.1 nm
VolumePorod 301 nm3

SASDFK4 – Condensin complex subunit 3-like protein, Ycg1, at 0.25mg/ml

Condensin complex subunit 3-like proteinCondensin complex subunit 3-like protein experimental SAS data
SASREF MX model
Sample: Condensin complex subunit 3-like protein monomer, 108 kDa Chaetomium thermophilum protein
Condensin complex subunit 3-like protein dimer, 217 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 20
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1. J Biol Chem 294(37):13822-13829 (2019)
Manalastas-Cantos K, Kschonsak M, Haering CH, Svergun DI
RgGuinier 4.6 nm
Dmax 15.0 nm
VolumePorod 280 nm3

SASDGL2 – Ring opening PaaZ from the phenylacetate degradation pathway (E. coli K12)

Bifunctional protein PaaZ experimental SAS data
OTHER model
Sample: Bifunctional protein PaaZ hexamer, 438 kDa Escherichia coli protein
Buffer: 25 mM HEPES, 50 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Feb 24
Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway. Nat Commun 10(1):4127 (2019)
Sathyanarayanan N, Cannone G, Gakhar L, Katagihallimath N, Sowdhamini R, Ramaswamy S, Vinothkumar KR
RgGuinier 6.2 nm
Dmax 20.0 nm
VolumePorod 636 nm3