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42 hits found for idp

SASDD62 – Microtubule associated protein MAP2c (isoform 3); 12 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 8.3 nm

SASDD72 – Microtubule associated protein MAP2c (isoform 3); 6 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 7.9 nm

SASDD82 – Microtubule associated protein MAP2c (isoform 3); 3 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 6.9 nm

SASDD92 – Microtubule associated protein MAP2c (isoform 3); 1.5 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 6.7 nm

SASDDA2 – Phosphorylated Microtubule associated protein MAP2c (isoform 3); 13.6 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 7.9 nm

SASDDB2 – Phosphorylated Microtubule associated protein MAP2c (isoform 3); 6.8 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: 50 mM MOPS, 150 mM NaCl, 0.03% NaN3, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 7.3 nm

SASDDC2 – Phosphorylated Microtubule associated protein MAP2c (isoform 3); 1.7 mg/ml

Microtubule-associated protein 2, isoform 3 experimental SAS data
Microtubule-associated protein 2, isoform 3 Kratky plot
Sample: Microtubule-associated protein 2, isoform 3 monomer, 49 kDa Rattus norvegicus protein
Buffer: MOPS map2c buffer, pH: 6.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 21
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J Biol Chem 293(34):13297-13309 (2018)
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
RgGuinier 6.7 nm

SASDED2 – Polyglutamine tract-binding protein 1 (PQBP-1)

Polyglutamine-binding protein 1 experimental SAS data
Polyglutamine tract-binding protein 1 (PQBP-1) Rg histogram
Sample: Polyglutamine-binding protein 1 monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1mM DTT,, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III on 2009 Nov 18
Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. Biophys J 102(7):1608-16 (2012)
Rees M, Gorba C, de Chiara C, Bui TT, Garcia-Maya M, Drake AF, Okazawa H, Pastore A, Svergun D, Chen YW
RgGuinier 3.7 nm
Dmax 13.0 nm
VolumePorod 51 nm3

SASDEH2 – Unlabeled nucleoporin NUP49/NSP49 (N49) without denaturant

Nucleoporin NUP49/NSP49 experimental SAS data
Unlabeled nucleoporin NUP49/NSP49 (N49) without denaturant Rg histogram
Sample: Nucleoporin NUP49/NSP49 monomer, 4 kDa Saccharomyces cerevisiae protein
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 1.6 nm
Dmax 6.0 nm
VolumePorod 4 nm3

SASDEJ2 – Labeled nucleoporin NUP49/NSP49 (N49-Alexa488/Alexa594) without denaturant

Nucleoporin NUP49/NSP49Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Nucleoporin NUP49/NSP49 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Nucleoporin NUP49/NSP49 monomer, 4 kDa Saccharomyces cerevisiae protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 1.9 nm
Dmax 6.5 nm
VolumePorod 12 nm3

SASDEK2 – Unlabeled nucleoporin NUP49/NSP49 (N49) with denaturant

Nucleoporin NUP49/NSP49 experimental SAS data
Unlabeled nucleoporin NUP49/NSP49 (N49) with denaturant Rg histogram
Sample: Nucleoporin NUP49/NSP49 monomer, 4 kDa Saccharomyces cerevisiae protein
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 1.7 nm
Dmax 6.5 nm
VolumePorod 4 nm3

SASDEL2 – Labeled nucleoporin NUP49/NSP49 (N49-Alexa488/Alexa594) with denaturant

Nucleoporin NUP49/NSP49Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Nucleoporin NUP49/NSP49 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Nucleoporin NUP49/NSP49 monomer, 4 kDa Saccharomyces cerevisiae protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.1 nm
Dmax 7.7 nm
VolumePorod 7 nm3

SASDEM2 – Unlabeled Nuclear Localization Signal (NLS) from the inner nuclear membrane protein HEH2 without denaturant

Inner nuclear membrane protein HEH2 experimental SAS data
Unlabeled Nuclear Localization Signal (NLS) from the inner nuclear membrane protein HEH2 without denaturant Rg histogram
Sample: Inner nuclear membrane protein HEH2 monomer, 5 kDa Saccharomyces cerevisiae protein
Buffer: 25 mM HEPES, 150 mM NaCl, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 25
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.4 nm
Dmax 11.6 nm
VolumePorod 16 nm3

SASDEN2 – Labeled Nuclear Localization Signal from the inner nuclear membrane protein HEH2 (NLS-Alexa488/Alexa594) without denaturant

Inner nuclear membrane protein HEH2Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Inner nuclear membrane protein HEH2 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Inner nuclear membrane protein HEH2 monomer, 5 kDa Saccharomyces cerevisiae protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: 25 mM HEPES, 150 mM NaCl, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 25
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.0 nm
Dmax 7.3 nm
VolumePorod 10 nm3

SASDEP2 – Unlabeled Nuclear Localization Signal (NLS) from the inner nuclear membrane protein HEH2 with denaturant

Inner nuclear membrane protein HEH2 experimental SAS data
Unlabeled Nuclear Localization Signal (NLS) from the inner nuclear membrane protein HEH2 with denaturant Rg histogram
Sample: Inner nuclear membrane protein HEH2 monomer, 5 kDa Saccharomyces cerevisiae protein
Buffer: 25 mM HEPES, 150 mM NaCl, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 25
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.3 nm
Dmax 7.1 nm
VolumePorod 10 nm3

SASDEQ2 – Labeled Nuclear Localization Signal from the inner nuclear membrane protein HEH2 (NLS-Alexa488/Alexa594) with denaturant

Inner nuclear membrane protein HEH2Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Inner nuclear membrane protein HEH2 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Inner nuclear membrane protein HEH2 monomer, 5 kDa Saccharomyces cerevisiae protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: 25 mM HEPES, 150 mM NaCl, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 25
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.4 nm
Dmax 8.1 nm
VolumePorod 12 nm3

SASDER2 – Unlabeled Importin Beta Binding domain (IBB) from importin subunit alpha-1 without denaturant

Importin subunit alpha-1 experimental SAS data
Unlabeled Importin Beta Binding domain (IBB) from importin subunit alpha-1 without denaturant Rg histogram
Sample: Importin subunit alpha-1 monomer, 11 kDa Homo sapiens protein
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.2 nm
Dmax 11.5 nm
VolumePorod 30 nm3

SASDES2 – Labeled Importin Beta Binding Domain (IBB-Alexa488/Alexa594) from importin subunit alpha-1 without denaturant

Importin subunit alpha-1Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Importin subunit alpha-1 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Importin subunit alpha-1 monomer, 11 kDa Homo sapiens protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 9
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.9 nm
Dmax 13.7 nm
VolumePorod 29 nm3

SASDET2 – Unlabeled Importin Beta Binding Domain (IBB) from importin subunit alpha-1 with denaturant

Importin subunit alpha-1 experimental SAS data
Unlabeled Importin Beta Binding Domain (IBB) from importin subunit alpha-1 with denaturant Rg histogram
Sample: Importin subunit alpha-1 monomer, 11 kDa Homo sapiens protein
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.1 nm
Dmax 15.3 nm
VolumePorod 34 nm3

SASDEU2 – Labeled Importin Beta Binding Domain from importin subunit alpha-1 (IBB-Alexa488/Alexa594) with denaturant

Importin subunit alpha-1Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Importin subunit alpha-1 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Importin subunit alpha-1 monomer, 11 kDa Homo sapiens protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.2 nm
Dmax 13.3 nm
VolumePorod 29 nm3

SASDEV2 – Unlabeled nuclear pore complex protein Nup153 (NUS) without denaturant

Nuclear pore complex protein Nup153 experimental SAS data
Unlabeled nuclear pore complex protein Nup153 (NUS) without denaturant Rg histogram
Sample: Nuclear pore complex protein Nup153 monomer, 8 kDa Homo sapiens protein
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.5 nm
Dmax 9.2 nm
VolumePorod 15 nm3

SASDEW2 – Labeled nuclear pore complex protein Nup153 (NUS-Alexa488/Alexa594) without denaturant

Nuclear pore complex protein Nup153Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Nuclear pore complex protein Nup153 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Nuclear pore complex protein Nup153 monomer, 8 kDa Homo sapiens protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.5 nm
Dmax 9.7 nm
VolumePorod 17 nm3

SASDEX2 – Unlabeled nuclear pore complex protein Nup153 (NUS) with denaturant

Nuclear pore complex protein Nup153 experimental SAS data
Unlabeled nuclear pore complex protein Nup153 (NUS) with denaturant Rg histogram
Sample: Nuclear pore complex protein Nup153 monomer, 8 kDa Homo sapiens protein
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.1 nm
Dmax 11.0 nm
VolumePorod 26 nm3

SASDEY2 – Labeled nuclear pore complex protein Nup153 (NUS-Alexa488/Alexa594) with denaturant

Nuclear pore complex protein Nup153Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Nuclear pore complex protein Nup153 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Nuclear pore complex protein Nup153 monomer, 8 kDa Homo sapiens protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.9 nm
Dmax 10.8 nm
VolumePorod 19 nm3

SASDEZ2 – Unlabeled nuclear pore complex protein Nup153 (NUL) without denaturant

Nuclear pore complex protein Nup153 experimental SAS data
Unlabeled nuclear pore complex protein Nup153 (NUL) without denaturant Rg histogram
Sample: Nuclear pore complex protein Nup153 monomer, 12 kDa Homo sapiens protein
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.0 nm
Dmax 10.9 nm
VolumePorod 32 nm3

SASDE23 – Labeled nuclear pore complex protein Nup153 (NUL-Alexa488/Alexa594) without denaturant

Nuclear pore complex protein Nup153Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Nuclear pore complex protein Nup153 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Nuclear pore complex protein Nup153 monomer, 12 kDa Homo sapiens protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.1 nm
Dmax 12.0 nm
VolumePorod 24 nm3

SASDE33 – Unlabeled nuclear pore complex protein Nup153 (NUL) with denaturant

Nuclear pore complex protein Nup153 experimental SAS data
Unlabeled nuclear pore complex protein Nup153 (NUL) with denaturant Rg histogram
Sample: Nuclear pore complex protein Nup153 monomer, 12 kDa Homo sapiens protein
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.5 nm
Dmax 16.0 nm
VolumePorod 53 nm3

SASDE43 – Labeled nuclear pore complex protein Nup153 (NUL-Alexa488/Alexa594) with denaturant

Nuclear pore complex protein Nup153Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Nuclear pore complex protein Nup153 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Nuclear pore complex protein Nup153 monomer, 12 kDa Homo sapiens protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 27 nm3

SASDC53 – Colicin N Translocation domain

Colicin N Translocation domain experimental SAS data
Colicin N Translocation domain Rg histogram
Sample: Colicin N Translocation domain monomer, 10 kDa Escherichia coli protein
Buffer: 50 mM Na-Phosphate 300 mM NaCl, pH: 7.6
Experiment: SAXS data collected at BM29, ESRF on 2012 Jun 29
The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N. Biophys J 113(8):1673-1684 (2017)
Johnson CL, Solovyova AS, Hecht O, Macdonald C, Waller H, Grossmann JG, Moore GR, Lakey JH
RgGuinier 2.8 nm
Dmax 11.4 nm
VolumePorod 22 nm3

SASDE53 – Unlabeled dihydrolipoyllysine-residue succinyltransferase component (BBL) with denaturant

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex experimental SAS data
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex Kratky plot
Sample: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex monomer, 4 kDa Escherichia coli protein
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.1 nm
Dmax 8.3 nm
VolumePorod 41 nm3

SASDE63 – Labeled dihydrolipoyllysine-residue succinyltransferase component (BBL-Alexa488/Alexa594) with denaturant

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexAlexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex monomer, 4 kDa Escherichia coli protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.3 nm
Dmax 10.7 nm
VolumePorod 13 nm3

SASDE73 – Unlabeled cold shock protein (CSP) with denaturant

Cold shock-like protein experimental SAS data
Cold shock-like protein Kratky plot
Sample: Cold shock-like protein monomer, 7 kDa Thermotoga maritima protein
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Mar 16
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.5 nm
Dmax 11.5 nm
VolumePorod 17 nm3

SASDE83 – Labeled cold shock protein (CSP-Alexa488/Alexa594) with denaturant

Cold shock-like proteinAlexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Cold shock-like protein Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Cold shock-like protein monomer, 7 kDa Thermotoga maritima protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.2 nm
Dmax 8.3 nm
VolumePorod 9 nm3

SASDE93 – Unlabeled thioredoxin (TRX) with denaturant

Thioredoxin 1 experimental SAS data
Thioredoxin 1 Kratky plot
Sample: Thioredoxin 1 monomer, 12 kDa Escherichia coli protein
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.6 nm
Dmax 13.0 nm
VolumePorod 34 nm3

SASDEA3 – Labeled thioredoxin (TRX-Alexa488/Alexa594) with denaturant

Thioredoxin 1Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data
Thioredoxin 1 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot
Sample: Thioredoxin 1 monomer, 12 kDa Escherichia coli protein
Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa
Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer: PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 3.2 nm
Dmax 13.9 nm
VolumePorod 31 nm3

SASDEB3 – Unlabeled nuclear pore complex protein Nup98-Nup96 (N98) without denaturant

Nuclear pore complex protein Nup98-Nup96 experimental SAS data
Nuclear pore complex protein Nup98-Nup96 Kratky plot
Sample: Nuclear pore complex protein Nup98-Nup96 monomer, 15 kDa Homo sapiens protein
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 24
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 2.9 nm
Dmax 10.4 nm
VolumePorod 27 nm3

SASDEC3 – Unlabeled nucleoporin NSP1 (NSP) without denaturant

Nucleoporin NSP1 experimental SAS data
Nucleoporin NSP1 Kratky plot
Sample: Nucleoporin NSP1 monomer, 18 kDa Saccharomyces cerevisiae protein
Buffer: PBS, 10 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 24
Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA
RgGuinier 4.1 nm
Dmax 15.0 nm
VolumePorod 45 nm3

SASDCY4 – RNase E 603-850

RNase E 603-850 experimental SAS data
RNase E 603-850 Rg histogram
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 5
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 5.3 nm
Dmax 27.5 nm
VolumePorod 139 nm3

SASDJB5 – Nipah virus phosphoprotein, N-terminal amino acids 1-406 (PNT)

Phosphoprotein experimental SAS data
Nipah virus phosphoprotein, N-terminal amino acids 1-406 (PNT) Rg histogram
Sample: Phosphoprotein monomer, 45 kDa Nipah henipavirus protein
Buffer: 20 mM Tris-HCl, 0.3 M NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 May 3
Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. Sci Rep 10(1):19574 (2020)
Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S
RgGuinier 6.2 nm
Dmax 23.0 nm
VolumePorod 210 nm3

SASDDF6 – Myelin basic protein

Myelin basic protein experimental SAS data
Myelin basic protein Rg histogram
Sample: Myelin basic protein monomer, 18 kDa Bos taurus protein
Buffer: 20 mM NaH2PO4/ Na2HPO4, 99.9% D2O, pH: 4.8
Experiment: SAXS data collected at BM29, ESRF on 2013 Feb 21
Internal nanosecond dynamics in the intrinsically disordered myelin basic protein. J Am Chem Soc 136(19):6987-94 (2014)
Stadler AM, Stingaciu L, Radulescu A, Holderer O, Monkenbusch M, Biehl R, Richter D
RgGuinier 3.3 nm
Dmax 11.1 nm

SASDBZ6 – Draxin

Draxin experimental SAS data
Draxin Rg histogram
Sample: Draxin monomer, 45 kDa Homo sapiens protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Aug 19
Structural Basis for Draxin-Modulated Axon Guidance and Fasciculation by Netrin-1 through DCC. Neuron 97(6):1261-1267.e4 (2018)
Liu Y, Bhowmick T, Liu Y, Gao X, Mertens HDT, Svergun DI, Xiao J, Zhang Y, Wang JH, Meijers R
RgGuinier 4.2 nm
Dmax 15.0 nm
VolumePorod 87 nm3

SASDCY9 – Oxidised chloroplastic calvin cycle protein CP12 from C. reinhardtii

Calvin cycle protein CP12, chloroplastic experimental SAS data
Oxidised chloroplastic calvin cycle protein CP12 from C. reinhardtii Rg histogram
Sample: Calvin cycle protein CP12, chloroplastic monomer, 11 kDa Chlamydomonas reinhardtii protein
Buffer: 50 mM phosphate buffer, 50 mM NaCl, 20 mM oxidized DTT, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Nov 3
Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase. J Mol Biol 430(8):1218-1234 (2018)
Launay H, Barré P, Puppo C, Zhang Y, Maneville S, Gontero B, Receveur-Bréchot V
RgGuinier 2.3 nm
Dmax 10.0 nm
VolumePorod 22 nm3