Browse by MODEL: Ab initio only

SASDBW7 – N-terminal and chromo-ATPase-DBD domains of chromo domain-containing protein 1 (Chd1: 1-1305)

chromodomain helicase DNA binding domain experimental SAS data
GASBOR model
Sample: Chromodomain helicase DNA binding domain monomer, 150 kDa Saccharomyces cerevisiae protein
Buffer: 50mM Hepes 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 30
Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
RgGuinier 4.9 nm
Dmax 16.0 nm
VolumePorod 340 nm3

SASDBX7 – Chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010)

chromodomain helicase DNA binding domain experimental SAS data
GASBOR model
Sample: Chromodomain helicase DNA binding domain monomer, 102 kDa Saccharomyces cerevisiae protein
Buffer: 50mM Hepes 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 30
Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
RgGuinier 4.1 nm
Dmax 16.1 nm
VolumePorod 190 nm3

SASDBY7 – N-terminal and chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 1-1010)

chromodomain helicase DNA binding domain experimental SAS data
GASBOR model
Sample: Chromodomain helicase DNA binding domain monomer, 117 kDa Saccharomyces cerevisiae protein
Buffer: 50mM Hepes 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 30
Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
RgGuinier 4.5 nm
Dmax 12.0 nm
VolumePorod 228 nm3

SASDBA7 – Human NEI like DNA glycosylase 1 (NEIL1) bound to Proliferating Cell Nuclear Antigen (PCNA) and DNA

Endonuclease 8-like 1dsDNAProliferating cell nuclear antigen experimental SAS data
DAMMIN model
Sample: Endonuclease 8-like 1 monomer, 45 kDa Homo sapiens protein
DsDNA monomer, 2 kDa DNA
Proliferating cell nuclear antigen monomer, 30 kDa Homo sapiens protein
Buffer: 25mM HEPES 100mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jan 20
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 45(5):2897-2909 (2017)
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.4 nm
Dmax 16.4 nm
VolumePorod 113 nm3

SASDBB7 – Human NEI like DNA glycosylase 1 (NEIL1) bound to DNA

Endonuclease 8-like 1dsDNA experimental SAS data
DAMMIN model
Sample: Endonuclease 8-like 1 monomer, 45 kDa Homo sapiens protein
DsDNA monomer, 2 kDa DNA
Buffer: 25mM HEPES 100mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jan 20
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 45(5):2897-2909 (2017)
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.3 nm
Dmax 17.5 nm
VolumePorod 92 nm3

SASDBC7 – Human NEI like DNA glycosylase 1 (NEIL1)

Endonuclease 8-like 1 experimental SAS data
GASBOR model
Sample: Endonuclease 8-like 1 monomer, 45 kDa Homo sapiens protein
Buffer: 25mM HEPES 300mM NaCl 1mM DTT 10% Glycerol, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Mar 13
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 45(5):2897-2909 (2017)
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.6 nm
Dmax 15.0 nm
VolumePorod 81 nm3

SASDBD7 – Human Proliferating Cell Nuclear Antigen (PCNA)

Proliferating cell nuclear antigen experimental SAS data
GASBOR model
Sample: Proliferating cell nuclear antigen trimer, 89 kDa Homo sapiens protein
Buffer: 25mM HEPES 100mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jan 20
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 45(5):2897-2909 (2017)
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.4 nm
Dmax 9.7 nm
VolumePorod 128 nm3

SASDBF7 – Dps2, DNA binding protein under starvation conditions (SEC-SAXS)

N-terminal truncated DNA protection during starvation protein 2 experimental SAS data
EOM/RANCH model
Sample: N-terminal truncated DNA protection during starvation protein 2 dodecamer, 279 kDa Deinococcus radiodurans R1 protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV
RgGuinier 4.2 nm
Dmax 12.7 nm
VolumePorod 445 nm3

SASDBG7 – Dps1, DNA binding protein under starvation conditions (SEC-SAXS)

DNA protection during starvation protein 1 experimental SAS data
GASBOR model
Sample: DNA protection during starvation protein 1 dodecamer, 276 kDa Deinococcus radiodurans R1 protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV
RgGuinier 4.2 nm
Dmax 12.8 nm
VolumePorod 437 nm3

SASDBH7 – Dps1 truncated, DNA binding protein under starvation conditions (SEC-SAXS)

N-terminal truncated DNA protection during starvation protein 1 experimental SAS data
GASBOR model
Sample: N-terminal truncated DNA protection during starvation protein 1 dodecamer, 216 kDa Deinococcus radiodurans R1 protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV
RgGuinier 3.9 nm
Dmax 10.0 nm
VolumePorod 291 nm3