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28 hits found for Fuertes

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

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