Browse by MODEL: Ab initio only

SASDNR3 – Fibrillin-1 fragment PF3

Fibrillin-1 PF3 experimental SAS data
DAMMIF model
Sample: Fibrillin-1 PF3 monomer, 78 kDa Homo sapiens protein
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 12
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 5.4 nm
Dmax 24.0 nm
VolumePorod 141 nm3

SASDNS3 – Latent-transforming growth factor beta-binding protein 1 C-terminus

Latent-transforming growth factor beta-binding protein 1 experimental SAS data
DAMMIF model
Sample: Latent-transforming growth factor beta-binding protein 1 monomer, 44 kDa Homo sapiens protein
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 12
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 4.7 nm
Dmax 20.5 nm
VolumePorod 102 nm3

SASDNT3 – Fibrillin-1 fragment PF3 crosslinked to latent transforming growth factor-beta-binding protein 1 C-terminus by transglutaminase 2

Latent-transforming growth factor beta-binding protein 1Fibrillin-1 PF3 experimental SAS data
DAMMIF model
Sample: Latent-transforming growth factor beta-binding protein 1 monomer, 44 kDa Homo sapiens protein
Fibrillin-1 PF3 monomer, 78 kDa Homo sapiens protein
Buffer: 10 mM Hepes, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 20
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 7.4 nm
Dmax 29.6 nm
VolumePorod 759 nm3

SASDN95 – Truncated Kelch13-R539T mutant

Kelch protein K13 (Truncated Kelch13-R539T, artemisinin-resistant mutation) experimental SAS data
GASBOR model
Sample: Kelch protein K13 (Truncated Kelch13-R539T, artemisinin-resistant mutation) hexamer, 396 kDa Plasmodium falciparum (isolate … protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR - Institute of Microbial Technology (IMTech) on 2020 Jul 25
Plasmodium falciparum Kelch13 and its artemisinin-resistant mutants assemble as hexamers in solution: a SAXS data driven modeling study. FEBS J (2022)
Goel N, Dhiman K, Kalidas N, Mukhopadhyay A, Ashish F, Bhattacharjee S
RgGuinier 6.6 nm
Dmax 20.5 nm
VolumePorod 1600 nm3

SASDNA5 – Truncated Kelch13-C580Y mutant

Kelch protein K13 (Truncated Kelch13-C580Y ) experimental SAS data
GASBOR model
Sample: Kelch protein K13 (Truncated Kelch13-C580Y ) hexamer, 397 kDa Plasmodium falciparum (isolate … protein
Buffer: Phosphate Buffer Saline, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR - Institute of Microbial Technology (IMTech) on 2020 Jul 28
Plasmodium falciparum Kelch13 and its artemisinin-resistant mutants assemble as hexamers in solution: a SAXS data driven modeling study. FEBS J (2022)
Goel N, Dhiman K, Kalidas N, Mukhopadhyay A, Ashish F, Bhattacharjee S
RgGuinier 6.4 nm
Dmax 18.4 nm
VolumePorod 1800 nm3

SASDNB5 – Truncated Kelch13-A578S mutant

Kelch protein K13 (Truncated Kelch13-A578S) experimental SAS data
GASBOR model
Sample: Kelch protein K13 (Truncated Kelch13-A578S) hexamer, 396 kDa Plasmodium falciparum (isolate … protein
Buffer: Phosphate Buffer Saline, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR - Institute of Microbial Technology (IMTech) on 2020 Jul 29
Plasmodium falciparum Kelch13 and its artemisinin-resistant mutants assemble as hexamers in solution: a SAXS data driven modeling study. FEBS J (2022)
Goel N, Dhiman K, Kalidas N, Mukhopadhyay A, Ashish F, Bhattacharjee S
RgGuinier 6.1 nm
Dmax 16.8 nm
VolumePorod 1700 nm3

SASDNF3 – Lectin nano-block dimer of WA20-H-ACG

Lectin nano-block WA20-H-ACG experimental SAS data
DAMMIN model
Sample: Lectin nano-block WA20-H-ACG dimer, 59 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5% glycerol,, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Oct 31
Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans International Journal of Molecular Sciences 23(2):676 (2022)
Irumagawa S, Hiemori K, Saito S, Tateno H, Arai R
RgGuinier 3.9 nm
Dmax 18.1 nm
VolumePorod 85 nm3

SASDNG3 – Lectin nano-block dimer of WA20-ΔN3ACG

Lectin nano-block WA20-ΔN3ACG experimental SAS data
DAMMIN model
Sample: Lectin nano-block WA20-ΔN3ACG dimer, 58 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5% glycerol,, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Oct 31
Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans International Journal of Molecular Sciences 23(2):676 (2022)
Irumagawa S, Hiemori K, Saito S, Tateno H, Arai R
RgGuinier 4.1 nm
Dmax 21.6 nm
VolumePorod 87 nm3

SASDLP2 – Outer membrane associated protein, FopA dimer in Tris-HCl, NaCl and n-Dodecyl beta-D-maltoside

Francisella tularensis outer membrane protein A experimental SAS data
Sample: Francisella tularensis outer membrane protein A dimer, 80 kDa Francisella tularensis subsp. … protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.05% B-DDM, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Mar 20
Structural and biophysical properties of FopA, a major outer membrane protein of Francisella tularensis. PLoS One 17(8):e0267370 (2022)
Nagaratnam N, Martin-Garcia JM, Yang JH, Goode MR, Ketawala G, Craciunescu FM, Zook JD, Sonowal M, Williams D, Grant TD, Fromme R, Hansen DT, Fromme P
RgGuinier 4.4 nm
Dmax 16.0 nm
VolumePorod 330 nm3

SASDNA3 – Association of the CPAP N-termini coiled-coil domain with the CP110 C-termini coiled-coil region

centrosomal-P4.1-associated-proteinCentriolar coiled-coil protein of 110 kDa experimental SAS data
DAMMIF model
Sample: Centrosomal-P4.1-associated-protein monomer, 12 kDa Homo sapiens protein
Centriolar coiled-coil protein of 110 kDa dimer, 20 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH 7.5, 100 mM NaCl, 1 mM DTT, 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 23
Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends. J Cell Biol 224(3) (2025)
Iyer SS, Chen F, Ogunmolu FE, Moradi S, Volkov VA, van Grinsven EJ, van Hoorn C, Wu J, Andrea N, Hua S, Jiang K, Vakonakis I, Potočnjak M, Herzog F, Gigant B, Gudimchuk N, Stecker KE, Dogterom M, Steinmetz MO, Akhmanova A
RgGuinier 3.5 nm
Dmax 12.2 nm
VolumePorod 35 nm3