SASBDB entries for UniProt ID:

SASDQ39 – SARS-CoV-2 spike protein ACE2 receptor binding domain (RBD) - reservoir sample storage with liquid jet delivery measured using XFEL

UniProt ID: P0DTC2 (319-566) Spike glycoprotein (ACE2 receptor binding domain)
Spike glycoprotein (ACE2 receptor binding domain) experimental SAS data
Spike glycoprotein (ACE2 receptor binding domain) Kratky plot
Sample: Spike glycoprotein (ACE2 receptor binding domain) monomer, 29 kDa Severe acute respiratory … protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SANS data collected at SPB/SFX, European XFEL on 2021 May 14
Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS). Commun Biol 6(1):1057 (2023)
Blanchet CE, Round A, Mertens HDT, Ayyer K, Graewert M, Awel S, Franke D, Dörner K, Bajt S, Bean R, Custódio TF, de Wijn R, Juncheng E, Henkel A, Gruzinov A, Jeffries CM, Kim Y, Kirkwood H, Kloos M, Knoška J, Koliyadu J, Letrun R, Löw C, Makroczyova J, Mall A, Meijers R, Pena Murillo GE, Oberthür D, Round E, Seuring C, Sikorski M, Vagovic P, Valerio J, Wollweber T, Zhuang Y, Schulz J, Haas H, Chapman HN, Mancuso AP, Svergun D
RgGuinier 3.0 nm

SASDQ49 – His-Tagged full length DNA repair protein RAD52 homolog

UniProt ID: P43351 (1-418) DNA repair protein RAD52 homolog
DNA repair protein RAD52 homolog experimental SAS data
His-Tagged full length DNA repair protein RAD52 homolog Rg histogram
Sample: DNA repair protein RAD52 homolog undecamer, 528 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 7.5, 250 mM NaCl, 1% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2022 Jul 21
An integrative structural study of the human full-length RAD52 at 2.2 Å resolution Communications Biology 7(1) (2024)
Balboni B, Marotta R, Rinaldi F, Milordini G, Varignani G, Girotto S, Cavalli A
RgGuinier 8.0 nm
Dmax 40.2 nm
VolumePorod 1218 nm3

SASDQB9 – YdaT_toxin domain-containing protein

UniProt ID: A0A6M7H0F8 (2-141) YdaT_toxin domain-containing protein
YdaT_toxin domain-containing protein experimental SAS data
OTHER [STATIC IMAGE] model
Sample: YdaT_toxin domain-containing protein tetramer, 74 kDa Escherichia coli O157:H7 protein
Buffer: 20 mM Tris-HCl, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2022 Apr 16
Structural basis of DNA binding by YdaT, a functional equivalent of the CII repressor in the cryptic prophage CP-933P from Escherichia coli O157:H7 Acta Crystallographica Section D Structural Biology 79(3):245-258 (2023)
Prolič-Kalinšek M, Volkov A, Hadži S, Van Dyck J, Bervoets I, Charlier D, Loris R
RgGuinier 3.5 nm
Dmax 12.0 nm
VolumePorod 130 nm3

SASDQC9 – Mutant YdaT_toxin domain-containing protein (L111N/F118R)

UniProt ID: A0A6M7H0F8 (2-141) YdaT_toxin domain-containing protein (mutant: L111N, F118R)
YdaT_toxin domain-containing protein (mutant: L111N, F118R) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: YdaT_toxin domain-containing protein (mutant: L111N, F118R) monomer, 18 kDa Escherichia coli O157:H7 protein
Buffer: 20 mM Tris-HCl, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Apr 14
Structural basis of DNA binding by YdaT, a functional equivalent of the CII repressor in the cryptic prophage CP-933P from Escherichia coli O157:H7 Acta Crystallographica Section D Structural Biology 79(3):245-258 (2023)
Prolič-Kalinšek M, Volkov A, Hadži S, Van Dyck J, Bervoets I, Charlier D, Loris R
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 32 nm3

SASDQD9 – N-terminal domain of YdaT_toxin domain-containing protein

UniProt ID: A0A6M7H0F8 (2-96) YdaT_toxin domain-containing protein
YdaT_toxin domain-containing protein experimental SAS data
OTHER [STATIC IMAGE] model
Sample: YdaT_toxin domain-containing protein monomer, 13 kDa Escherichia coli O157:H7 protein
Buffer: 20 mM Tris-HCl, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2022 Apr 16
Structural basis of DNA binding by YdaT, a functional equivalent of the CII repressor in the cryptic prophage CP-933P from Escherichia coli O157:H7 Acta Crystallographica Section D Structural Biology 79(3):245-258 (2023)
Prolič-Kalinšek M, Volkov A, Hadži S, Van Dyck J, Bervoets I, Charlier D, Loris R
RgGuinier 1.7 nm
Dmax 5.7 nm
VolumePorod 29 nm3

SASDQE9 – YdaT_toxin domain-containing protein bound to 30 base pair dsDNA

UniProt ID: A0A6M7H0F8 (2-141) YdaT_toxin domain-containing protein

UniProt ID: None (None-None) Om 30 base pair dsDNA
YdaT_toxin domain-containing proteinOm 30 base pair dsDNA experimental SAS data
OTHER model
Sample: YdaT_toxin domain-containing protein tetramer, 74 kDa Escherichia coli O157:H7 protein
Om 30 base pair dsDNA dimer, 37 kDa DNA
Buffer: 20 mM Tris-HCl, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 14
Structural basis of DNA binding by YdaT, a functional equivalent of the CII repressor in the cryptic prophage CP-933P from Escherichia coli O157:H7 Acta Crystallographica Section D Structural Biology 79(3):245-258 (2023)
Prolič-Kalinšek M, Volkov A, Hadži S, Van Dyck J, Bervoets I, Charlier D, Loris R
RgGuinier 4.2 nm
Dmax 12.8 nm
VolumePorod 190 nm3

SASDQF9 – GRP94 protein (Endoplasmin)

UniProt ID: P08113 (22-754) Endoplasmin
Endoplasmin experimental SAS data
Endoplasmin Kratky plot
Sample: Endoplasmin dimer, 169 kDa Mus musculus protein
Buffer: 25 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Jul 11
Visualization of conformational transition of GRP94 in solution. Life Sci Alliance 7(2) (2024)
Sun S, Zhu R, Zhu M, Wang Q, Li N, Yang B
RgGuinier 5.6 nm
Dmax 24.0 nm
VolumePorod 260 nm3

SASDQG9 – GRP94 protein (Endoplasmin) bound to ADP

UniProt ID: P08113 (22-754) Endoplasmin
Endoplasmin experimental SAS data
Endoplasmin Kratky plot
Sample: Endoplasmin dimer, 169 kDa Mus musculus protein
Buffer: 25 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Jul 11
Visualization of conformational transition of GRP94 in solution. Life Sci Alliance 7(2) (2024)
Sun S, Zhu R, Zhu M, Wang Q, Li N, Yang B
RgGuinier 5.7 nm
Dmax 24.0 nm
VolumePorod 274 nm3

SASDQH9 – GRP94 protein (Endoplasmin) bound to AMP-PNP

UniProt ID: P08113 (22-754) Endoplasmin
Endoplasmin experimental SAS data
Endoplasmin Kratky plot
Sample: Endoplasmin dimer, 169 kDa Mus musculus protein
Buffer: 25 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Jul 11
Visualization of conformational transition of GRP94 in solution. Life Sci Alliance 7(2) (2024)
Sun S, Zhu R, Zhu M, Wang Q, Li N, Yang B
RgGuinier 5.5 nm
Dmax 24.5 nm
VolumePorod 260 nm3

SASDQJ9 – An assembly between C-terminal truncated Netrin UNC-6 and the extracellular domain of Netrin receptor UNC-5 with porcine intestinal mucosa heparin (UNC-6ΔC-heparin-UNC-5 ECD complex)

UniProt ID: P34710 (22-461) Netrin unc-6

UniProt ID: Q26261-1 (1-331) Isoform a of Netrin receptor unc-5

UniProt ID: None (None-None) Heparin, porcine intestinal mucosa
Netrin unc-6Isoform a of Netrin receptor unc-5Heparin, porcine intestinal mucosa experimental SAS data
Netrin unc-6 Isoform a of Netrin receptor unc-5 Heparin, porcine intestinal mucosa Kratky plot
Sample: Netrin unc-6 monomer, 52 kDa Caenorhabditis elegans protein
Isoform a of Netrin receptor unc-5 monomer, 38 kDa Caenorhabditis elegans protein
Heparin, porcine intestinal mucosa monomer, 15 kDa Sus scrofa domesticus
Buffer: 10 mM HEPES pH 7.2, 150 mM NaCl, 100 mM MgSO4, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Jun 18
Structural insights into the formation of repulsive netrin guidance complexes. Sci Adv 10(7):eadj8083 (2024)
Priest JM, Nichols EL, Smock RG, Hopkins JB, Mendoza JL, Meijers R, Shen K, Özkan E
RgGuinier 10.4 nm
Dmax 37.3 nm
VolumePorod 2156 nm3