SASBDB entries for UniProt ID:

SASDMT8 – Sulfite reductase flavoprotein-60/deuterated-hemoprotein heterodimer in 41% D2O

UniProt ID: P17846 (1-570) Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)

UniProt ID: P38038 (53-599) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein)
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at EQ-SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 2.2 nm
Dmax 6.6 nm

SASDMU8 – Sulfite reductase flavoprotein-60/deuterated-hemoprotein heterodimer in 86% D2O

UniProt ID: P17846 (1-570) Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)

UniProt ID: P38038 (53-599) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein)
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at EQ-SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 3.1 nm
Dmax 12.4 nm

SASDMV8 – Sulfite reductase flavoprotein-60/deuterated-hemoprotein heterodimer in 100% D2O

UniProt ID: P17846 (1-570) Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)

UniProt ID: P38038 (53-599) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein)
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at EQ-SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 4.0 nm
Dmax 13.9 nm

SASDM79 – Lysozyme crystallization solutions with precipitants from crystallization kits CS 1 and CS2 (mixture of monomers, dimers and octamers, with octamer volume fractions from 0 to 0.7%)

UniProt ID: P00698 (19-129) Lysozyme C
Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 100 mM HEPES pH 7.5, 20 %(v/v) jeffamine M-600, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 28
Dependence of concentration of precursor clusters formed in lysozyme crystallization solutions on degree of supersaturation and its effect on character of solution transition from liquid to condensed phase
Petr Konarev
RgGuinier 1.8 nm

SASDM89 – Lysozyme crystallization solutions with precipitants from crystallization kits CS 1 and CS2 (mixture of monomers, dimers and octamers, with octamer volume fractions from 0.9% to 4.4%)

UniProt ID: P00698 (19-129) Lysozyme C
Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 100 mM sodium acetate, pH 4.6, 2.0 M sodium formate, pH: 4.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 28
Dependence of concentration of precursor clusters formed in lysozyme crystallization solutions on degree of supersaturation and its effect on character of solution transition from liquid to condensed phase
Petr Konarev
RgGuinier 2.2 nm

SASDM99 – Lysozyme crystallization solutions with precipitants from crystallization kits CS 1 and CS2 (mixture of monomers, dimers and octamers, with octamer volume fractions from 4.9% to 21.1%)

UniProt ID: P00698 (19-129) Lysozyme C
Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 200 mM K/Na tartrate, 100 mM tri-sodium citrate pH 5.6, 2.0 M ammonium sulfate, pH: 5.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 28
Dependence of concentration of precursor clusters formed in lysozyme crystallization solutions on degree of supersaturation and its effect on character of solution transition from liquid to condensed phase
Petr Konarev
RgGuinier 2.4 nm

SASDMA9 – Diacetylchitobiose deacetylase (isolated hexamer from SEC-SAXS)

UniProt ID: A0A160VQZ8 (1-267) Diacetylchitobiose deacetylase
Diacetylchitobiose deacetylase experimental SAS data
PYMOL model
Sample: Diacetylchitobiose deacetylase hexamer, 186 kDa Thermococcus chitonophagus protein
Buffer: 20 mM TRIS, 200 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Sep 26
Structural, Thermodynamic and Enzymatic Characterization of N,N-Diacetylchitobiose Deacetylase from Pyrococcus chitonophagus. Int J Mol Sci 23(24) (2022)
Biniek-Antosiak K, Bejger M, Śliwiak J, Baranowski D, Mohammed ASA, Svergun DI, Rypniewski W
RgGuinier 3.6 nm
Dmax 11.2 nm
VolumePorod 317 nm3

SASDMB9 – Diacetylchitobiose deacetylase (oligomeric mixture of hexamers and dodecamers)

UniProt ID: A0A160VQZ8 (1-267) Diacetylchitobiose deacetylase
Diacetylchitobiose deacetylase experimental SAS data
PYMOL model
Sample: Diacetylchitobiose deacetylase, 185 kDa Thermococcus chitonophagus protein
Buffer: 20 mM TRIS, 200 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Sep 26
Structural, Thermodynamic and Enzymatic Characterization of N,N-Diacetylchitobiose Deacetylase from Pyrococcus chitonophagus. Int J Mol Sci 23(24) (2022)
Biniek-Antosiak K, Bejger M, Śliwiak J, Baranowski D, Mohammed ASA, Svergun DI, Rypniewski W
RgGuinier 3.9 nm

SASDMG9 – Multidrug resistance operon repressor (MexR) of the MexAB-OprM multidrug efflux pump operon of Pseudomonas aeruginosa

UniProt ID: P52003 (5-139) Multidrug resistance operon repressor
Multidrug resistance operon repressor experimental SAS data
DAMFILT model
Sample: Multidrug resistance operon repressor dimer, 32 kDa Pseudomonas aeruginosa protein
Buffer: 20mM HEPES, 150mM NaCl, 10mM DTT, 1% v/v glycerol, pH: 7.1
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Nov 23
Small-angle X-ray and neutron scattering of MexR and its complex with DNA supports a conformational selection binding model Biophysical Journal (2022)
Caporaletti F, Pietras Z, Morad V, Mårtensson L, Gabel F, Wallner B, Martel A, Sunnerhagen M
RgGuinier 2.3 nm
Dmax 7.7 nm
VolumePorod 56 nm3

SASDMH9 – Pseudomonas aeruginosa Multidrug resistance operon repressor (MexR) in complex with 34bp dsDNA binding sequence (SANS data at 0% D2O)

UniProt ID: P52003 (5-139) Multidrug resistance operon repressor

UniProt ID: None (None-None) 34 base pair double-stranded DNA
Multidrug resistance operon repressor34 base pair double-stranded DNA experimental SAS data
MONSA model
Sample: Multidrug resistance operon repressor dimer, 32 kDa Pseudomonas aeruginosa protein
34 base pair double-stranded DNA monomer, 21 kDa synthetic construct DNA
Buffer: 20mM NaPO4, 150 mM NaCl, 10 mM DTT, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 May 30
Small-angle X-ray and neutron scattering of MexR and its complex with DNA supports a conformational selection binding model Biophysical Journal (2022)
Caporaletti F, Pietras Z, Morad V, Mårtensson L, Gabel F, Wallner B, Martel A, Sunnerhagen M
RgGuinier 2.9 nm
Dmax 7.8 nm
VolumePorod 79 nm3