Browse by MODEL: Ab initio only

SASDVE2 – Human Haemoglobin (Sigma-Aldrich) with 10% PEG2000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml

Hemoglobin subunit alphaHemoglobin subunit betaProtoporphyrin IX containing fe experimental SAS data
DAMMIF model
Sample: Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein
Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Protoporphyrin IX containing fe monomer, 1 kDa
Buffer: 100mM Sodium Phosphate buffer with 10% (w/v) PEG2000, pH: 7
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Oct 6
Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications The Journal of Physical Chemistry B (2024)
Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B
RgGuinier 2.8 nm
Dmax 11.3 nm
VolumePorod 131 nm3

SASDVZ5 – Human DNA repair protein RAD52 homolog (amino acids 1-212)

DNA repair protein RAD52 homolog experimental SAS data
DAMMIF model
Sample: DNA repair protein RAD52 homolog decamer, 234 kDa Homo sapiens protein
Buffer: 20 mM Bis-Tris, 10% glycerol, 400 mM NaCl, 100 mM KCl, 1 mM EDTA, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS 1000, Eppley Structural Biology Facility, University of Nebraska Medical Center on 2014 Jul 25
A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52 Journal of Structural Biology 216(3):108115 (2024)
Struble L, Lovelace J, Borgstahl G
RgGuinier 4.1 nm
Dmax 11.8 nm
VolumePorod 375 nm3

SASDV26 – Human DNA repair protein RAD52 homolog (amino acids 1-303)

DNA repair protein RAD52 homolog experimental SAS data
DAMMIF model
Sample: DNA repair protein RAD52 homolog nonamer, 300 kDa Homo sapiens protein
Buffer: 20 mM Bis-Tris, 10% GLycerol, 400 mM NaCl, 100 mM KCl, 1mM EDTA, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS 1000, Eppley Structural Biology Facility, University of Nebraska Medical Center on 2014 Jul 25
A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52 Journal of Structural Biology 216(3):108115 (2024)
Struble L, Lovelace J, Borgstahl G
RgGuinier 4.8 nm
Dmax 18.3 nm
VolumePorod 782 nm3

SASDMN3 – Wild type E3 ubiquitin-protein ligase LRSAM1

E3 ubiquitin-protein ligase LRSAM1 experimental SAS data
DAMFILT model
Sample: E3 ubiquitin-protein ligase LRSAM1 monomer, 84 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl pH 8.0, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2019 Dec 7
Leucine Rich Repeat And Sterile Alpha Motif Containing 1 (LRSAM1)
Si Hoon Park
RgGuinier 6.1 nm
Dmax 19.4 nm
VolumePorod 250 nm3

SASDMP3 – Wild type E3 ubiquitin-protein ligase LRSAM1 (1-632): C-terminal PTAP/PSAP motif and RING domain deletion mutant, ΔPTAP/PSAP-RING

E3 ubiquitin-protein ligase LRSAM1 - ΔPTAP/PSAP-RING experimental SAS data
DAMFILT model
Sample: E3 ubiquitin-protein ligase LRSAM1 - ΔPTAP/PSAP-RING monomer, 74 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl pH 8.0, 300 mM NaCl, 1 mM TCEP, 5% w/v glycerol, pH: 8
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2017 Oct 24
Leucine Rich Repeat And Sterile Alpha Motif Containing 1 (LRSAM1)
Si Hoon Park
RgGuinier 5.5 nm
Dmax 18.0 nm
VolumePorod 322 nm3

SASDMQ3 – Wild type E3 ubiquitin-protein ligase LRSAM1 (1-307): N-terminal LRR containing domain

E3 ubiquitin-protein ligase LRSAM1 - LRR containing N-terminal domain experimental SAS data
DAMFILT model
Sample: E3 ubiquitin-protein ligase LRSAM1 - LRR containing N-terminal domain monomer, 35 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl pH 8.0, 300 mM NaCl, 1 mM TCEP, 5% w/v glycerol, pH: 8
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2017 Oct 23
Leucine Rich Repeat And Sterile Alpha Motif Containing 1 (LRSAM1)
Si Hoon Park
RgGuinier 3.4 nm
Dmax 8.2 nm
VolumePorod 105 nm3

SASDMR3 – Wild type E3 ubiquitin-protein ligase LRSAM1 (561-632): SAM domain

E3 ubiquitin-protein ligase LRSAM1 - SAM domain experimental SAS data
DAMFILT model
Sample: E3 ubiquitin-protein ligase LRSAM1 - SAM domain monomer, 8 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl pH 8.0, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2019 Apr 4
Leucine Rich Repeat And Sterile Alpha Motif Containing 1 (LRSAM1)
Si Hoon Park
RgGuinier 1.4 nm
Dmax 4.3 nm
VolumePorod 11 nm3

SASDMS3 – Wild type E3 ubiquitin-protein ligase LRSAM1 (80-171): domains LRR3-6 in the Repebody scaffold

E3 ubiquitin-protein ligase LRSAM1 experimental SAS data
DAMFILT model
Sample: E3 ubiquitin-protein ligase LRSAM1 monomer, 30 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl pH 8.0, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2019 Apr 4
Leucine Rich Repeat And Sterile Alpha Motif Containing 1 (LRSAM1)
Si Hoon Park
RgGuinier 2.5 nm
Dmax 8.3 nm
VolumePorod 43 nm3

SASDU84 – Calcium-gelsolin and the G-form of actin at a 1:2 molar ratio in low ionic strength (SEC-SAXS)

GelsolinActin, cytoplasmic 1 experimental SAS data
GASBOR model
Sample: Gelsolin monomer, 84 kDa Homo sapiens protein
Actin, cytoplasmic 1 monomer, 42 kDa Gallus gallus protein
Buffer: 2 mM Tris-Cl, pH 8.0, 0.2 mM ATP, 1 mM NaN3, 0.1 mM CaCl2, 0.5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Aug 31
Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes. Int J Biol Macromol :134556 (2024)
Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish
RgGuinier 4.4 nm
Dmax 25.0 nm
VolumePorod 241 nm3

SASDU94 – Calcium-gelsolin and the G-form of actin at a 1:1 molar ratio in low ionic strength (SEC-SAXS)

GelsolinActin, cytoplasmic 1 experimental SAS data
GASBOR model
Sample: Gelsolin monomer, 84 kDa Homo sapiens protein
Actin, cytoplasmic 1 monomer, 42 kDa Gallus gallus protein
Buffer: 2 mM Tris-Cl, pH 8.0, 0.2 mM ATP, 1 mM NaN3, 0.1 mM CaCl2, 0.5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 1
Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes. Int J Biol Macromol :134556 (2024)
Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish
RgGuinier 4.6 nm
Dmax 25.0 nm
VolumePorod 243 nm3