SASBDB entries for UniProt ID:

SASDFL7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, 2H acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) in 42% v/v D2O

UniProt ID: P53853 (1-225) Vacuolar protein sorting-associated protein 75 (1-225 aa)

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data
GROMACS model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.4 nm
Dmax 10.5 nm

SASDFM7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, acetylatransferase Rtt109, 2H histone chaperone Vps75 (1-225aa) in 42% v/v D2O

UniProt ID: P53853 (1-225) Vacuolar protein sorting-associated protein 75 (1-225 aa)

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 2.7 nm
Dmax 9.0 nm

SASDFN7 – Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4, histone chaperones Asf1 and Vps75 (1-225aa) (acquired in 100% v/v D2O)

UniProt ID: P53853 (1-225) Vacuolar protein sorting-associated protein 75 (1-225 aa)

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Kratky plot
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 May 30
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.5 nm
Dmax 11.0 nm

SASDFP7 – Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4 and histone chaperones Asf1 and Vps75, all full-length, acquired in 100% v/v D2O

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length

UniProt ID: P53853 (1-264) Vacuolar protein sorting-associated protein 75 full-length
Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-lengthVacuolar protein sorting-associated protein 75 full-length experimental SAS data
Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Vacuolar protein sorting-associated protein 75 full-length Kratky plot
Sample: Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.5 nm
Dmax 11.5 nm

SASDFQ7 – Complex with 1H histone chaperone Vps75, histones H3 and H4, 2H histone chaperone Asf1, histone acetyltransferase Rtt109, acquired in 42% v/v D2O

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length

UniProt ID: P53853 (1-264) Vacuolar protein sorting-associated protein 75 full-length
Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-lengthVacuolar protein sorting-associated protein 75 full-length experimental SAS data
Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Vacuolar protein sorting-associated protein 75 full-length Kratky plot
Sample: Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.1 nm
Dmax 9.5 nm

SASDFR7 – Rabbit muscle fructose-bisphosphate aldolase A, K229M mutant

UniProt ID: P00883 (2-364) Fructose-bisphosphate aldolase A
Fructose-bisphosphate aldolase A experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Fructose-bisphosphate aldolase A tetramer, 157 kDa Oryctolagus cuniculus protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, Département de Biochimie, Université de Montréal on 2019 Jun 14
Rabbit muscle fructose-1,6-bisphosphate aldolase K229M mutant
Normand Cyr
RgGuinier 3.6 nm
Dmax 11.8 nm
VolumePorod 213 nm3

SASDFS7 – Talin-1 head amino acids 1-405(Δ139-168)

UniProt ID: Q9Y490 (1-405) Talin-1 (Δ139-168), human
Talin-1 (Δ139-168), human experimental SAS data
Talin-1 head amino acids 1-405(Δ139-168) Rg histogram
Sample: Talin-1 (Δ139-168), human monomer, 48 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate, 150mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Sep 24
The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. J Cell Sci 133(19) (2020)
Kukkurainen S, Azizi L, Zhang P, Jacquier MC, Baikoghli M, von Essen M, Tuukkanen A, Laitaoja M, Liu X, Rahikainen R, Orłowski A, Jänis J, Määttä JAE, Varjosalo M, Vattulainen I, Róg T, Svergun D, Cheng RH, Wu J, Hytönen VP, Wehrle-Haller B
RgGuinier 3.3 nm
Dmax 13.3 nm
VolumePorod 77 nm3

SASDFT7 – Talin-1 head amino acids 1-405

UniProt ID: Q9Y490 (1-405) Talin-1, human
Talin-1, human experimental SAS data
Talin-1 head amino acids 1-405 Rg histogram
Sample: Talin-1, human monomer, 51 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Sep 24
The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. J Cell Sci 133(19) (2020)
Kukkurainen S, Azizi L, Zhang P, Jacquier MC, Baikoghli M, von Essen M, Tuukkanen A, Laitaoja M, Liu X, Rahikainen R, Orłowski A, Jänis J, Määttä JAE, Varjosalo M, Vattulainen I, Róg T, Svergun D, Cheng RH, Wu J, Hytönen VP, Wehrle-Haller B
RgGuinier 3.4 nm
Dmax 11.5 nm
VolumePorod 94 nm3

SASDFU7 – Talin-1 head amino acids 1-405(Δ134-170/GAG insert)

UniProt ID: Q9Y490 (1-405) Talin-1 (Δ134-170/GAG insert), human
Talin-1 (Δ134-170/GAG insert), human experimental SAS data
Talin-1 head amino acids 1-405(Δ134-170/GAG insert) Rg histogram
Sample: Talin-1 (Δ134-170/GAG insert), human monomer, 47 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate, 150mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Sep 24
The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. J Cell Sci 133(19) (2020)
Kukkurainen S, Azizi L, Zhang P, Jacquier MC, Baikoghli M, von Essen M, Tuukkanen A, Laitaoja M, Liu X, Rahikainen R, Orłowski A, Jänis J, Määttä JAE, Varjosalo M, Vattulainen I, Róg T, Svergun D, Cheng RH, Wu J, Hytönen VP, Wehrle-Haller B
RgGuinier 3.0 nm
Dmax 10.2 nm
VolumePorod 71 nm3

SASDFZ7 – Full-length myotilin with N-terminally fused thioredoxin tag

UniProt ID: Q9UBF9 (2-498) his-trx-myotilin
his-trx-myotilin experimental SAS data
Full-length myotilin with N-terminally fused thioredoxin tag Rg histogram
Sample: His-trx-myotilin monomer, 70 kDa Homo sapiens protein
Buffer: 20 mM Tris, 400 mM NaCl, 250 mM arginine, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jun 11
Molecular basis of F-actin regulation and sarcomere assembly via myotilin PLOS Biology 19(4):e3001148 (2021)
Kostan J, Pavšič M, Puž V, Schwarz T, Drepper F, Molt S, Graewert M, Schreiner C, Sajko S, van der Ven P, Onipe A, Svergun D, Warscheid B, Konrat R, Fürst D, Lenarčič B, Djinović-Carugo K, Machesky L
RgGuinier 5.1 nm
Dmax 16.7 nm
VolumePorod 131 nm3