SASBDB entries for UniProt ID:

SASDSY9 – SARS-CoV-2 N-protein (N1-245, residues 1-245) L223P, L227P and L230P triple mutant: 400 µM

UniProt ID: P0DTC9 (1-245) Nucleoprotein (L223P, L227P, L230P)
Nucleoprotein (L223P, L227P, L230P) experimental SAS data
Nucleoprotein (L223P, L227P, L230P) Kratky plot
Sample: Nucleoprotein (L223P, L227P, L230P) monomer, 27 kDa Severe acute respiratory … protein
Buffer: 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Jan 29
SARS-CoV-2 N-protein variants: N1-246 and IDL176-246
Guillem Hernandez
RgGuinier 4.6 nm
Dmax 19.0 nm
VolumePorod 75 nm3

SASDTC3 – Teneurin-3 A0B1 isoform in 2 mM calcium - 0.36 mg/mL

UniProt ID: Q9WTS6-3 (343-2706) Isoform A0B1 of Teneurin-3
Isoform A0B1 of Teneurin-3 experimental SAS data
Isoform A0B1 of Teneurin-3 Kratky plot
Sample: Isoform A0B1 of Teneurin-3 dimer, 545 kDa Mus musculus protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM CaCl2, pH: 7.8
Experiment: SAXS data collected at BM29, ESRF on 2022 Sep 10
Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition Nature Communications 15(1) (2024)
Gogou C, Beugelink J, Frias C, Kresik L, Jaroszynska N, Drescher U, Janssen B, Hindges R, Meijer D
RgGuinier 7.8 nm
Dmax 30.0 nm
VolumePorod 1022 nm3

SASDFT5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 6.5 with 50 mM NaCl

UniProt ID: None (None-None) 80bp_DNA Forward

UniProt ID: None (None-None) 80bp_DNA Reverse

UniProt ID: P0ACF0 (1-90) DNA-binding protein HU-alpha
80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, 10 kDa Escherichia coli protein
Buffer: 10mM Bis-Tris, 50 mM NaCl, pH: 6.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDL94 – Human Albumin (P5)

UniProt ID: P02768 (None-None) Albumin
Albumin experimental SAS data
Albumin Kratky plot
Sample: Albumin monomer, 69 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 1
Albumin in patients with liver disease shows an altered conformation. Commun Biol 4(1):731 (2021)
Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M
RgGuinier 2.9 nm
Dmax 8.9 nm

SASDLB8 – The Fe–S cluster assembly 1 homolog of pigeon (retention time at the magnet position No.5 : 30 min)

UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
Iron-sulfur cluster assembly 1 homolog, mitochondrial experimental SAS data
Iron-sulfur cluster assembly 1 homolog, mitochondrial Kratky plot
Sample: Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
Buffer: 20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Nov 30
Magnetic field effects on the structure and molecular behavior of pigeon iron–sulfur protein Protein Science 31(6) (2022)
Arai S, Shimizu R, Adachi M, Hirai M
RgGuinier 5.4 nm
Dmax 19.0 nm

SASDM82 – Ubiquitin-fold modifier 1

UniProt ID: P61960 (1-83) Ubiquitin fold modifer 1
Ubiquitin fold modifer 1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ubiquitin fold modifer 1 monomer, 9 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jun 13
Structure and dynamics of UBA5-UFM1 complex formation showing new insights in the UBA5 activation mechanism Journal of Structural Biology :107796 (2021)
Fuchs S, Kikhney A, Schubert R, Kaiser C, Liebau E, Svergun D, Betzel C, Perbandt M
RgGuinier 1.5 nm
Dmax 5.1 nm
VolumePorod 16 nm3

SASDTE3 – Teneurin-3 A1B0 isoform - 0.69 mg/mL

UniProt ID: Q9WTS6-4 (343-2708) Isoform A1B0 of Teneurin-3
Isoform A1B0 of Teneurin-3 experimental SAS data
Isoform A1B0 of Teneurin-3 Kratky plot
Sample: Isoform A1B0 of Teneurin-3 dimer, 541 kDa Mus musculus protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at BM29, ESRF on 2022 Sep 10
Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition Nature Communications 15(1) (2024)
Gogou C, Beugelink J, Frias C, Kresik L, Jaroszynska N, Drescher U, Janssen B, Hindges R, Meijer D
RgGuinier 9.0 nm
Dmax 34.0 nm
VolumePorod 1042 nm3

SASDFU5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 6.5 with 100 mM NaCl

UniProt ID: None (None-None) 80bp_DNA Forward

UniProt ID: None (None-None) 80bp_DNA Reverse

UniProt ID: P0ACF0 (1-90) DNA-binding protein HU-alpha
80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 14-mer, 133 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 6.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.2 nm
Dmax 24.4 nm
VolumePorod 274 nm3

SASDLA4 – Human Albumin (P6)

UniProt ID: P02768 (None-None) Albumin
Albumin experimental SAS data
Albumin Kratky plot
Sample: Albumin monomer, 69 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 1
Albumin in patients with liver disease shows an altered conformation. Commun Biol 4(1):731 (2021)
Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M
RgGuinier 2.8 nm
Dmax 8.5 nm

SASDLC8 – The Fe–S cluster assembly 1 homolog of pigeon (retention time at the magnet position No.5 : 60 min)

UniProt ID: P0DN75 (2-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
Iron-sulfur cluster assembly 1 homolog, mitochondrial experimental SAS data
Iron-sulfur cluster assembly 1 homolog, mitochondrial Kratky plot
Sample: Iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
Buffer: 20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Nov 30
Magnetic field effects on the structure and molecular behavior of pigeon iron–sulfur protein Protein Science 31(6) (2022)
Arai S, Shimizu R, Adachi M, Hirai M
RgGuinier 5.7 nm
Dmax 21.2 nm