SASBDB entries for UniProt ID:

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

UniProt ID: P49790 (1313-1390) Nuclear pore complex protein Nup153

UniProt ID: None (None-None) Alexa Fluor™ 594 C5 Maleimide

UniProt ID: None (None-None) Alexa Fluor™ 488 C5 Hydroxylamine
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

UniProt ID: P49790 (884-993) Nuclear pore complex protein Nup153
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

UniProt ID: P49790 (884-993) Nuclear pore complex protein Nup153

UniProt ID: None (None-None) Alexa Fluor™ 594 C5 Maleimide

UniProt ID: None (None-None) Alexa Fluor™ 488 C5 Hydroxylamine
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

UniProt ID: P49790 (884-993) Nuclear pore complex protein Nup153
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

UniProt ID: P49790 (884-993) Nuclear pore complex protein Nup153

UniProt ID: None (None-None) Alexa Fluor™ 594 C5 Maleimide

UniProt ID: None (None-None) Alexa Fluor™ 488 C5 Hydroxylamine
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

UniProt ID: P0AFG6 (115-151) Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
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

UniProt ID: P0AFG6 (115-151) Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

UniProt ID: None (None-None) Alexa Fluor™ 594 C5 Maleimide

UniProt ID: None (None-None) Alexa Fluor™ 488 C5 Hydroxylamine
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

UniProt ID: O54310 (3-58) Cold shock-like protein
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

UniProt ID: O54310 (3-58) Cold shock-like protein

UniProt ID: None (None-None) Alexa Fluor™ 594 C5 Maleimide

UniProt ID: None (None-None) Alexa Fluor™ 488 C5 Hydroxylamine
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

UniProt ID: P0AA25 (2-106) Thioredoxin 1
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