Browse by MODEL: Ab initio only

SASDQ68 – Minimal proline dehydrogenase domain of proline utilization A (SmPutADeltaAlpha2) 3.4 mg/mL

Minimal proline dehydrogenase domain of proline utilization A (design #2) experimental SAS data
OTHER model
Sample: Minimal proline dehydrogenase domain of proline utilization A (design #2) dimer, 87 kDa Sinorhizobium meliloti protein
Buffer: 25 mM HEPES pH 7.6, 150 mM NaCl, and 1mM TCEP, pH: 7.6
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2022 Apr 12
Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery. Protein Eng Des Sel (2022)
Bogner AN, Ji J, Tanner JJ
RgGuinier 3.0 nm
Dmax 9.8 nm
VolumePorod 108 nm3

SASDPM4 – Apo SH2-SH3-SH2 domains from p120RasGAP

Ras GTPase-activating protein 1 experimental SAS data
DAMMIF model
Sample: Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8 350 mM NaCl 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Dec 12
Tandem engagement of phosphotyrosines by the dual SH2 domains of p120RasGAP. Structure (2022)
Stiegler AL, Vish KJ, Boggon TJ
RgGuinier 2.6 nm
Dmax 10.3 nm
VolumePorod 41 nm3

SASDFE6 – Sliding beta clamp

Beta sliding clamp experimental SAS data
GASBOR model
Sample: Beta sliding clamp dimer, 86 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris pH 8.0, 200 mM NaCl , 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 15
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex International Journal of Biological Macromolecules (2022)
Shukla A, Afsar M, Khanam T, Kumar N, Ali F, Kumar S, Jahan F, Ramachandran R
RgGuinier 3.7 nm
Dmax 10.3 nm
VolumePorod 186 nm3

SASDFF6 – Probable exodeoxyribonuclease III protein XthA, sliding beta clamp complex

Beta sliding clampProbable exodeoxyribonuclease III protein XthA (Exonuclease III) (EXO III) (AP endonuclease VI) experimental SAS data
DAMMIF model
Sample: Beta sliding clamp dimer, 86 kDa Mycobacterium tuberculosis protein
Probable exodeoxyribonuclease III protein XthA (Exonuclease III) (EXO III) (AP endonuclease VI) monomer, 33 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 15
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex International Journal of Biological Macromolecules (2022)
Shukla A, Afsar M, Khanam T, Kumar N, Ali F, Kumar S, Jahan F, Ramachandran R
RgGuinier 3.5 nm
Dmax 11.3 nm
VolumePorod 98 nm3

SASDFG6 – Probable exodeoxyribonuclease III protein XthA, sliding beta clamp, DNA ligase-A tricomplex

Beta sliding clampProbable exodeoxyribonuclease III protein XthADNA ligase A experimental SAS data
DAMMIF model
Sample: Beta sliding clamp dimer, 86 kDa Mycobacterium tuberculosis protein
Probable exodeoxyribonuclease III protein XthA monomer, 31 kDa Mycobacterium tuberculosis protein
DNA ligase A monomer, 76 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 17
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex International Journal of Biological Macromolecules (2022)
Shukla A, Afsar M, Khanam T, Kumar N, Ali F, Kumar S, Jahan F, Ramachandran R
RgGuinier 5.8 nm
Dmax 25.3 nm
VolumePorod 501 nm3

SASDFH6 – Probable exodeoxyribonuclease III protein XthA, sliding beta clamp, DNA ligase-A tricomplex in the presence of DNA substrate

Probable exodeoxyribonuclease III protein XthADNA ligase ABeta sliding clampDNA ligase A nicked DNA substrate experimental SAS data
DAMMIF model
Sample: Probable exodeoxyribonuclease III protein XthA monomer, 31 kDa Mycobacterium tuberculosis protein
DNA ligase A monomer, 76 kDa Mycobacterium tuberculosis protein
Beta sliding clamp dimer, 86 kDa Mycobacterium tuberculosis protein
DNA ligase A nicked DNA substrate dimer, 16 kDa DNA
Buffer: 50 mM Tris pH 8.0, 200 mM NaCl , 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 17
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex International Journal of Biological Macromolecules (2022)
Shukla A, Afsar M, Khanam T, Kumar N, Ali F, Kumar S, Jahan F, Ramachandran R
RgGuinier 5.8 nm
Dmax 19.1 nm
VolumePorod 496 nm3

SASDQG6 – N-terminal truncation mutant of the periplasmic region of conjugal transfer mating pair stabilization protein TraG* from the R100 plasmid

Conjugal transfer mating pair stabilization protein TraG experimental SAS data
DAMMIF model
Sample: Conjugal transfer mating pair stabilization protein TraG monomer, 52 kDa Shigella flexneri 4c protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5% glycerol, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 23
Solution characterization of the dynamic conjugative entry exclusion protein TraG Structural Dynamics 9(6):064702 (2022)
Bragagnolo N, Audette G
RgGuinier 4.1 nm
Dmax 17.5 nm
VolumePorod 130 nm3

SASDQH6 – Periplasmic region of the conjugal transfer mating pair stabilization protein TraG* from the R100 plasmid

Conjugal transfer mating pair stabilization protein TraG experimental SAS data
DAMMIF model
Sample: Conjugal transfer mating pair stabilization protein TraG monomer, 57 kDa Shigella flexneri 4c protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5% glycerol, 0.05% NP40, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 23
Solution characterization of the dynamic conjugative entry exclusion protein TraG Structural Dynamics 9(6):064702 (2022)
Bragagnolo N, Audette G
RgGuinier 5.8 nm
Dmax 45.0 nm

SASDQQ5 – Oligomerisation domain of phosphoprotein from Borna disease virus

Phosphoprotein experimental SAS data
DAMMIF model
Sample: Phosphoprotein tetramer, 47 kDa Borna disease virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.5 nm
Dmax 17.0 nm
VolumePorod 66 nm3

SASDQR5 – Oligomerisation domain of phosphoprotein from Munia bornavirus

Phosphoprotein oligomerisation domain experimental SAS data
DAMMIF model
Sample: Phosphoprotein oligomerisation domain tetramer, 50 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.6 nm
Dmax 17.8 nm
VolumePorod 70 nm3