Browse by MODEL: No model

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)

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

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

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

SASDER7 – KRAB-associated protein 1 (KAP1); TRIM28, amino acids 23-812

Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28; amino acids 23-812 experimental SAS data
Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28; amino acids 23-812 Kratky plot
Sample: Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28; amino acids 23-812 dimer, 175 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 500 mM NaCl, 10 % Glycerol, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 6
KAP1 is an antiparallel dimer with a functional asymmetry. Life Sci Alliance 2(4) (2019)
Fonti G, Marcaida MJ, Bryan LC, Träger S, Kalantzi AS, Helleboid PJ, Demurtas D, Tully MD, Grudinin S, Trono D, Fierz B, Dal Peraro M
RgGuinier 8.9 nm
Dmax 38.0 nm
VolumePorod 853 nm3

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

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

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

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

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

SASDFD8 – Histidine-binding periplasmic protein (HisBP), apo-form

Histidine-binding periplasmic protein experimental SAS data
Histidine-binding periplasmic protein Kratky plot
Sample: Histidine-binding periplasmic protein monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.0 nm
Dmax 6.0 nm
VolumePorod 32 nm3

SASDFE8 – Histidine-binding periplasmic protein (HisBP) in the presence of histidine - His-bound 5-fold excess

Histidine-binding periplasmic protein experimental SAS data
Histidine-binding periplasmic protein Kratky plot
Sample: Histidine-binding periplasmic protein monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 1.8 nm
Dmax 5.7 nm
VolumePorod 33 nm3