SASBDB entries for UniProt ID:

SASDJA4 – Endonuclease VIII from E. coli (size exclusion chromatography SAXS)

UniProt ID: P50465 (2-263) Endonuclease 8

Endonuclease 8 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Endonuclease 8 monomer, 31 kDa Escherichia coli protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, 2% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Mar 9
Unique Structural Features of Mammalian NEIL2 DNA Glycosylase Prime Its Activity for Diverse DNA Substrates and Environments. Structure (2020)
Eckenroth BE, Cao VB, Averill AM, Dragon JA, Doublié S
RgGuinier 2.3 nm
Dmax 7.8 nm
VolumePorod 45 nm3

SASDJB4 – Endonuclease VIII - Like 2 from Monodelphis domestica (size exclusion chromatography SAXS) full length

UniProt ID: F7AMK3 (3-336) Nei like DNA glycosylase 2

Nei like DNA glycosylase 2 experimental SAS data
Nei like DNA glycosylase 2 Kratky plot
Sample: Nei like DNA glycosylase 2 monomer, 39 kDa Monodelphis domestica protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, 2% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Mar 9
Unique Structural Features of Mammalian NEIL2 DNA Glycosylase Prime Its Activity for Diverse DNA Substrates and Environments. Structure (2020)
Eckenroth BE, Cao VB, Averill AM, Dragon JA, Doublié S
RgGuinier 2.7 nm
Dmax 8.2 nm
VolumePorod 58 nm3

SASDJC4 – Endonuclease VIII - Like 2 from Monodelphis domestica (size exclusion chromatography SAXS) MdoNEIL2 cut (Δ67-133)

UniProt ID: F7AMK3 (None-None) Nei like DNA glycosylase 2 (Δ67-133)

Nei like DNA glycosylase 2 (Δ67-133) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Nei like DNA glycosylase 2 (Δ67-133) monomer, 33 kDa Monodelphis domestica protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, 2% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Mar 9
Unique Structural Features of Mammalian NEIL2 DNA Glycosylase Prime Its Activity for Diverse DNA Substrates and Environments. Structure (2020)
Eckenroth BE, Cao VB, Averill AM, Dragon JA, Doublié S
RgGuinier 2.4 nm
Dmax 7.8 nm
VolumePorod 47 nm3

SASDJD4 – Bacteriorhodopsin solubilized in contrast-matched octyl glucoside

UniProt ID: P02945 (14-262) Bacteriorhodopsin

Bacteriorhodopsin experimental SAS data
Bacteriorhodopsin Kratky plot
Sample: Bacteriorhodopsin monomer, 27 kDa Halobacterium salinarum protein
Buffer: 25 mM NaH2PO4, 1.35 mM KOH, 40 mM partially-deuterated octyl glucoside mixture, pH: 5.6
Experiment: SANS data collected at NGB 30m SANS, NIST Center for High Resolution Neutron Scattering (CHRNS) on 2017 Jan 20
Direct localization of detergents and bacteriorhodopsin in the lipidic cubic phase by small-angle neutron scattering IUCrJ 8(1) (2021)
Cleveland IV T, Blick E, Krueger S, Leung A, Darwish T, Butler P
RgGuinier 2.7 nm
Dmax 5.4 nm
VolumePorod 68 nm3

SASDJE4 – Bacteriorhodopsin in contrast-matched lipidic cubic phase formed with deuterated monoolein

UniProt ID: P02945 (14-262) Bacteriorhodopsin

Bacteriorhodopsin experimental SAS data
Bacteriorhodopsin Kratky plot
Sample: Bacteriorhodopsin monomer, 27 kDa Halobacterium salinarum protein
Buffer: 25 mM NaH2PO4, 1.35 mM KOH, 40 mM octyl glucoside, pH: 5.6
Experiment: SANS data collected at NG7, NIST Center for High Resolution Neutron Scattering (CHRNS) on 2017 May 15
Direct localization of detergents and bacteriorhodopsin in the lipidic cubic phase by small-angle neutron scattering IUCrJ 8(1) (2021)
Cleveland IV T, Blick E, Krueger S, Leung A, Darwish T, Butler P
RgGuinier 2.7 nm
Dmax 6.2 nm
VolumePorod 49 nm3

SASDJG4 – SARS-CoV-2 spike protein ACE2 receptor binding domain (RBD)

UniProt ID: P0DTC2 (319-566) Spike glycoprotein (ACE2 receptor binding domain)

Spike glycoprotein (ACE2 receptor binding domain) experimental SAS data
SASREF model
Sample: Spike glycoprotein (ACE2 receptor binding domain) monomer, 29 kDa Severe acute respiratory … protein
Buffer: 25 mM Tris 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 May 1
Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2 Nature Communications 11(1) (2020)
Custódio T, Das H, Sheward D, Hanke L, Pazicky S, Pieprzyk J, Sorgenfrei M, Schroer M, Gruzinov A, Jeffries C, Graewert M, Svergun D, Dobrev N, Remans K, Seeger M, McInerney G, Murrell B, Hällberg B, Löw C
RgGuinier 3.0 nm
Dmax 13.1 nm
VolumePorod 64 nm3

SASDJH4 – SARS-CoV-2 spike protein ACE2 receptor binding domain (RBD) bound to the synthetic nanobody Sybody 23 (Sy23)

UniProt ID: None (None-None) Synthetic nanobody Sybody 23

UniProt ID: P0DTC2 (319-566) Spike glycoprotein (ACE2 receptor binding domain)

Synthetic nanobody Sybody 23Spike glycoprotein (ACE2 receptor binding domain) experimental SAS data
CORAL model
Sample: Synthetic nanobody Sybody 23 monomer, 16 kDa synthetic construct protein
Spike glycoprotein (ACE2 receptor binding domain) monomer, 29 kDa Severe acute respiratory … protein
Buffer: 25 mM Tris 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 May 10
Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2 Nature Communications 11(1) (2020)
Custódio T, Das H, Sheward D, Hanke L, Pazicky S, Pieprzyk J, Sorgenfrei M, Schroer M, Gruzinov A, Jeffries C, Graewert M, Svergun D, Dobrev N, Remans K, Seeger M, McInerney G, Murrell B, Hällberg B, Löw C
RgGuinier 3.5 nm
Dmax 15.1 nm
VolumePorod 87 nm3

SASDJK4 – RNA polymerase core complex

UniProt ID: P9WGZ1 (1-347) DNA-directed RNA polymerase subunit alpha

UniProt ID: P9WGY9 (7-1178) DNA-directed RNA polymerase subunit beta

UniProt ID: P9WGY7 (2-1316) DNA-directed RNA polymerase subunit beta'

UniProt ID: P9WGY5 (2-110) DNA-directed RNA polymerase subunit omega

DNA-directed RNA polymerase subunit alphaDNA-directed RNA polymerase subunit betaDNA-directed RNA polymerase subunit beta'DNA-directed RNA polymerase subunit omega experimental SAS data
DAMFILT model
Sample: DNA-directed RNA polymerase subunit alpha dimer, 78 kDa Mycobacterium tuberculosis protein
DNA-directed RNA polymerase subunit beta monomer, 129 kDa Mycobacterium tuberculosis protein
DNA-directed RNA polymerase subunit beta' monomer, 147 kDa Mycobacterium tuberculosis protein
DNA-directed RNA polymerase subunit omega monomer, 12 kDa Mycobacterium tuberculosis protein
Buffer: 10 mM Tris-Cl, 100 mM NaCl, 10 mM MgCl2, 0.1 mM EDTA, 5% Glycerol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Mar 8
Structural and biochemical characterization of RNA polymerase core and UvrD complex: a key component in transcription coupled DNA repair
Ravishankar Ramachandran
RgGuinier 5.1 nm
Dmax 19.3 nm
VolumePorod 262 nm3

SASDJL4 – RNA polymerase core subunit in complex with ATP-dependent DNA helicase UvrD1

UniProt ID: P9WGZ1 (1-347) DNA-directed RNA polymerase subunit alpha

UniProt ID: P9WGY9 (7-1178) DNA-directed RNA polymerase subunit beta

UniProt ID: P9WGY7 (2-1316) DNA-directed RNA polymerase subunit beta'

UniProt ID: P9WGY5 (1-110) DNA-directed RNA polymerase subunit omega

UniProt ID: P9WMQ1 (1-771) ATP-dependent DNA helicase UvrD1

DNA-directed RNA polymerase subunit alphaDNA-directed RNA polymerase subunit betaDNA-directed RNA polymerase subunit beta'DNA-directed RNA polymerase subunit omegaATP-dependent DNA helicase UvrD1 experimental SAS data
DAMMIF model
Sample: DNA-directed RNA polymerase subunit alpha dimer, 75 kDa Mycobacterium tuberculosis protein
DNA-directed RNA polymerase subunit beta monomer, 129 kDa Mycobacterium tuberculosis protein
DNA-directed RNA polymerase subunit beta' monomer, 147 kDa Mycobacterium tuberculosis protein
DNA-directed RNA polymerase subunit omega monomer, 12 kDa Mycobacterium tuberculosis protein
ATP-dependent DNA helicase UvrD1 monomer, 85 kDa Mycobacterium tuberculosis protein
Buffer: 10 mM Tris-Cl, 100 mM NaCl, 10 mM MgCl2, 0.1 mM EDTA, 5% Glycerol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Mar 11
Structural and biochemical characterization of RNA polymerase core and UvrD complex: a key component in transcription coupled DNA repair
Ravishankar Ramachandran
RgGuinier 7.5 nm
Dmax 22.2 nm
VolumePorod 898 nm3

SASDJM4 – ATP-dependent DNA helicase UvrD1 (Apo-UvrD)

UniProt ID: P9WMQ1 (1-771) ATP-dependent DNA helicase UvrD1

ATP-dependent DNA helicase UvrD1 experimental SAS data
DAMFILT model
Sample: ATP-dependent DNA helicase UvrD1 monomer, 85 kDa Mycobacterium tuberculosis protein
Buffer: 10 mM Tris-Cl, 100 mM NaCl, 10 mM MgCl2, 0.1 mM EDTA, 5% Glycerol, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2020 Feb 28
Structural and biochemical characterization of RNA polymerase core and UvrD complex: a key component in transcription coupled DNA repair
Ravishankar Ramachandran
RgGuinier 3.4 nm
Dmax 8.4 nm
VolumePorod 132 nm3