SASBDB entries for UniProt ID:

SASDJN3 – Native alpha-2-macroglobulin, deglycosylated

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Alpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2019 Apr 12
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 7.6 nm
Dmax 20.2 nm

SASDJP3 – Methylamine-treated alpha-2-macroglobulin, deglcycosylated

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Alpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2019 Apr 13
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 19.7 nm

SASDJQ3 – Trypsin-treated alpha-2-macroglobulin, deglycosylated

UniProt ID: P00760 (1-246) Cationic trypsin

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Cationic trypsinAlpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Cationic trypsin dimer, 52 kDa Bos taurus protein
Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 20.7 nm

SASDJR3 – BceAB-type ABC-Transporter nucleotide-binding domain, SaNsrF

UniProt ID: Q8DZX1 (1-250) ABC transporter, ATP-binding protein (Nucleotide-Binding Domain SaNsrF)
ABC transporter, ATP-binding protein (Nucleotide-Binding Domain SaNsrF) experimental SAS data
OTHER model
Sample: ABC transporter, ATP-binding protein (Nucleotide-Binding Domain SaNsrF) monomer, 31 kDa Streptococcus agalactiae protein
Buffer: 100 mM HEPES, 150 mM NaCl, 10% glycerol, pH: 8
Experiment: SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2019 Dec 11
Characterization of the nucleotide-binding domain NsrF from the BceAB-type ABC-transporter NsrFP from the human pathogen Streptococcus agalactiae Scientific Reports 10(1) (2020)
Furtmann F, Porta N, Hoang D, Reiners J, Schumacher J, Gottstein J, Gohlke H, Smits S
RgGuinier 2.4 nm
Dmax 7.9 nm
VolumePorod 64 nm3

SASDJS3 – Adenylate cyclase toxin CyaA RTX block II-V

UniProt ID: P0DKX7 (1132-1681) Bifunctional hemolysin/adenylate cyclase
Bifunctional hemolysin/adenylate cyclase experimental SAS data
DAMMIF model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 57 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins. J Mol Biol (2020)
Motlova L, Klimova N, Fiser R, Sebo P, Bumba L
RgGuinier 4.0 nm
Dmax 13.3 nm
VolumePorod 94 nm3

SASDJT3 – Adenylate cyclase toxin CyaA RTX block III-V

UniProt ID: P0DKX7 (1243-1681) Bifunctional hemolysin/adenylate cyclase
Bifunctional hemolysin/adenylate cyclase experimental SAS data
DAMMIF model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 45 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins. J Mol Biol (2020)
Motlova L, Klimova N, Fiser R, Sebo P, Bumba L
RgGuinier 3.4 nm
Dmax 12.1 nm
VolumePorod 85 nm3

SASDJU3 – Adenylate cyclase toxin CyaA RTX block IV-V

UniProt ID: P0DKX7 (1372-1681) Bifunctional hemolysin/adenylate cyclase
Bifunctional hemolysin/adenylate cyclase experimental SAS data
DAMMIF model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 32 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins. J Mol Biol (2020)
Motlova L, Klimova N, Fiser R, Sebo P, Bumba L
RgGuinier 2.7 nm
Dmax 8.6 nm
VolumePorod 45 nm3

SASDJV3 – GTPase-Activation Protein (GAP) domain (73-204) of Vibrio cholerae Outer Protein E (VopE)

UniProt ID: A0A655XAV0 (73-204) Outer membrane virulence protein yopE
Outer membrane virulence protein yopE experimental SAS data
Outer membrane virulence protein yopE Kratky plot
Sample: Outer membrane virulence protein yopE monomer, 15 kDa Vibrio cholerae protein
Buffer: 10 mM HEPES-HCl, pH 7.4, 150 mM NaCl, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Jun 29
Solution structure and dynamics of the mitochondrial‐targeted GTPase ‐activating protein ( GAP ) VopE by an integrated NMR / SAXS approach Protein Science (2022)
Smith K, Lee W, Tonelli M, Lee Y, Light S, Cornilescu G, Chakravarthy S
RgGuinier 2.0 nm
Dmax 8.0 nm
VolumePorod 28 nm3

SASDJW3 – YraP from Acinetobacter baumannii full-length, minus signal-peptide and acyl anchoring cysteine

UniProt ID: V5VFJ0 (20-235) BON domain protein
BON domain protein experimental SAS data
DAMMIF model
Sample: BON domain protein decamer, 229 kDa Acinetobacter baumannii protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 11
BonA from Acinetobacter baumannii Forms a Divisome-Localized Decamer That Supports Outer Envelope Function. mBio :e0148021 (2021)
Grinter R, Morris FC, Dunstan RA, Leung PM, Kropp A, Belousoff M, Gunasinghe SD, Scott NE, Beckham S, Peleg AY, Greening C, Li J, Heinz E, Lithgow T
RgGuinier 4.7 nm
Dmax 16.4 nm
VolumePorod 546 nm3

SASDJX3 – YraP from Acinetobacter baumannii full-length, minus signal-peptide and 27 N-terminal amino acids

UniProt ID: V5VFJ0 (46-235) BON domain protein
BON domain protein experimental SAS data
DAMMIF model
Sample: BON domain protein monomer, 20 kDa Acinetobacter baumannii protein
Buffer: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 11
BonA from Acinetobacter baumannii Forms a Divisome-Localized Decamer That Supports Outer Envelope Function. mBio :e0148021 (2021)
Grinter R, Morris FC, Dunstan RA, Leung PM, Kropp A, Belousoff M, Gunasinghe SD, Scott NE, Beckham S, Peleg AY, Greening C, Li J, Heinz E, Lithgow T
RgGuinier 3.1 nm
Dmax 10.8 nm
VolumePorod 49 nm3