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

SASDBG6 – Ribosome biogenesis protein 15 (Nop15)

Ribosome biogenesis protein 15 experimental SAS data
EOM/RANCH model
Sample: Ribosome biogenesis protein 15 monomer, 17 kDa Saccharomyces cerevisiae protein
Buffer: 25 mM HEPES, 500 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Apr 25
Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. Nucleic Acids Res 45(5):2829-2837 (2017)
Zhang J, Gonzalez LE, Hall TMT
RgGuinier 2.4 nm
Dmax 10.3 nm
VolumePorod 38 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

SASDC83 – Dimeric apoptosis regulator BAX (Bcl-2 associated X)

Apoptosis regulator BAX (Bcl-2 associated X) experimental SAS data
CORAL model
Sample: Apoptosis regulator BAX (Bcl-2 associated X) dimer, 42 kDa Homo sapiens protein
Buffer: 20mM sodium phosphate 100mM NaCl, pH: 8
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2015 May 28
Oligomerization process of Bcl-2 associated X protein revealed from intermediate structures in solution. Phys Chem Chem Phys 19(11):7947-7954 (2017)
Shih O, Yeh YQ, Liao KF, Sung TC, Chiang YW, Jeng US
RgGuinier 3.0 nm
Dmax 9.5 nm
VolumePorod 86 nm3

SASDC93 – Tetrameric apoptosis regulator BAX (Bcl-2 associated X)

Apoptosis regulator BAX (Bcl-2 associated X) experimental SAS data
SASREF model
Sample: Apoptosis regulator BAX (Bcl-2 associated X) tetramer, 85 kDa Homo sapiens protein
Buffer: 20mM sodium phosphate 100mM NaCl, pH: 8
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2015 May 28
Oligomerization process of Bcl-2 associated X protein revealed from intermediate structures in solution. Phys Chem Chem Phys 19(11):7947-7954 (2017)
Shih O, Yeh YQ, Liao KF, Sung TC, Chiang YW, Jeng US
RgGuinier 3.6 nm
Dmax 12.0 nm
VolumePorod 180 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

4774 hits found.