SASBDB entries for UniProt ID:

SASDFE3 – Filamin A Ig-like domains 4-6, V711D mutant (FLNa4-6 V711D) at 4 mg/ml

UniProt ID: P21333 (574-869) Filamin A Ig-like domains 4-6, V711D mutation
Filamin A Ig-like domains 4-6, V711D mutation experimental SAS data
Filamin A Ig-like domains 4-6, V711D mutation Kratky plot
Sample: Filamin A Ig-like domains 4-6, V711D mutation monomer, 32 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 10
Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia. Biophys J 117(8):1467-1475 (2019)
Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
RgGuinier 4.1 nm
Dmax 15.0 nm
VolumePorod 64 nm3

SASDFF3 – Filamin A Ig-like domains 4-6, V711D mutant (FLNa4-6 V711D) at 2 mg/ml

UniProt ID: P21333 (574-869) Filamin A Ig-like domains 4-6, V711D mutation
Filamin A Ig-like domains 4-6, V711D mutation experimental SAS data
Filamin A Ig-like domains 4-6, V711D mutation Kratky plot
Sample: Filamin A Ig-like domains 4-6, V711D mutation monomer, 32 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 10
Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia. Biophys J 117(8):1467-1475 (2019)
Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
RgGuinier 4.0 nm
Dmax 14.8 nm
VolumePorod 57 nm3

SASDFG3 – Filamin A Ig-like domains 4-6, H743P mutant (FLNa4-6 H743P) at 4 mg/ml

UniProt ID: P21333 (574-869) Filamin A Ig-like domains 4-6, H743P mutation
Filamin A Ig-like domains 4-6, H743P mutation experimental SAS data
Filamin A Ig-like domains 4-6, H743P mutation Kratky plot
Sample: Filamin A Ig-like domains 4-6, H743P mutation monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 10
Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia. Biophys J 117(8):1467-1475 (2019)
Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
RgGuinier 4.3 nm
Dmax 16.0 nm
VolumePorod 70 nm3

SASDFH3 – Filamin A Ig-like domains 4-6, H743P mutant (FLNa4-6 H743P) at 2 mg/ml

UniProt ID: P21333 (574-869) Filamin A Ig-like domains 4-6, H743P mutation
Filamin A Ig-like domains 4-6, H743P mutation experimental SAS data
Filamin A Ig-like domains 4-6, H743P mutation Kratky plot
Sample: Filamin A Ig-like domains 4-6, H743P mutation monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 10
Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia. Biophys J 117(8):1467-1475 (2019)
Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
RgGuinier 4.0 nm
Dmax 15.3 nm
VolumePorod 60 nm3

SASDFJ3 – Maltose binding protein-SpoIVB peptidase fusion (MBP-SpoIVB)

UniProt ID: P17896 (None-None) SpoIVB peptidase (MBP fusion)
SpoIVB peptidase (MBP fusion) experimental SAS data
CHIMERA model
Sample: SpoIVB peptidase (MBP fusion) monomer, 80 kDa Bacillus subtilis protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 5% glycerol, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Jul 12
Solution Structure of SpoIVB Reveals Mechanism of PDZ Domain-Regulated Protease Activity. Front Microbiol 10:1232 (2019)
Xie X, Guo N, Xue G, Xie D, Yuan C, Harrison J, Li J, Jiang L, Huang M
RgGuinier 3.7 nm
Dmax 15.6 nm
VolumePorod 96 nm3

SASDFK3 – Splicing factor, proline- and glutamine-rich (SFPQ)

UniProt ID: P23246 (276-535) Splicing factor, proline- and glutamine-rich
Splicing factor, proline- and glutamine-rich experimental SAS data
CORAL model
Sample: Splicing factor, proline- and glutamine-rich dimer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 250 mM NaCl, 5% (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 19
A new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ. Acta Crystallogr F Struct Biol Commun 75(Pt 6):439-449 (2019)
Hewage TW, Caria S, Lee M
RgGuinier 2.8 nm
Dmax 8.2 nm
VolumePorod 91 nm3

SASDFL3 – All 1H histone acetyltransferase Rtt109 complex with histones H3 and H4 and histone chaperones Asf1 and Vps75 (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: P84233 (35-135) Histone H3.2 (35-135 aa)

UniProt ID: P62799 (1-103) Histone H4
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK 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 H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 3
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.5 nm
Dmax 11.8 nm

SASDFM3 – Complex with 1H histone chaperone Asf1 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1H Asf1-H3:H4, 2H Rtt109-Vps75) 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: P84233 (35-135) Histone H3.2 (35-135 aa)

UniProt ID: P62799 (1-103) Histone H4
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK 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 H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 4
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier -2.8 nm

SASDFN3 – Complex with 1H histone chaperones Asf1 and Vps75 and histones H3 and H4, 70%-2H histone acetyltransferase Rtt109 (1H Asf1-H3:H4-Vps75, 2H(70%) Rtt109) 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: P84233 (35-135) Histone H3.2 (35-135 aa)

UniProt ID: P62799 (1-103) Histone H4
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK 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 H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 4
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.3 nm
Dmax 10.5 nm

SASDFP3 – Complex with 1H histone chaperone Asf1, acetyltransferase Rtt109 and histones H3 and H4, 70%-2H histone chaperone Vps75 (1H Asf1-H3:H4-Rtt109, 2H(70%) Vps75) 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: P84233 (35-135) Histone H3.2 (35-135 aa)

UniProt ID: P62799 (1-103) Histone H4
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK 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 H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 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 29
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 2.8 nm
Dmax 9.5 nm