Browse by MODEL: Ensemble

SASDC33 – Colicin N delta 1-39

Colicin N delta 1-39 experimental SAS data
Colicin N delta 1-39 Rg histogram
Sample: Colicin N delta 1-39 monomer, 39 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 2.7 nm
Dmax 9.0 nm
VolumePorod 60 nm3

SASDC43 – Colicin K145A mutant

Colicin N K145A mutant experimental SAS data
Colicin K145A mutant Rg histogram
Sample: Colicin N K145A mutant monomer, 43 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 3.2 nm
Dmax 13.6 nm
VolumePorod 68 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

SASDCM6 – Small GTPase Rab5 conjugated with ubiquitin at K116

Monoubiquitinated Rab5 at K165 experimental SAS data
Small GTPase Rab5 conjugated with ubiquitin at K116 Rg histogram
Sample: Monoubiquitinated Rab5 at K165 monomer, 32 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 10 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2016 Nov 21
Site-specific monoubiquitination downregulates Rab5 by disrupting effector binding and guanine nucleotide conversion. Elife 6 (2017)
Shin D, Na W, Lee JH, Kim G, Baek J, Park SH, Choi CY, Lee S
RgGuinier 2.6 nm
Dmax 8.7 nm

SASDCN6 – Small GTPase Rab5 conjugated with ubiquitin at K140

Monoubiquitinated Rab5 at K165 experimental SAS data
Small GTPase Rab5 conjugated with ubiquitin at K140 Rg histogram
Sample: Monoubiquitinated Rab5 at K165 monomer, 32 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 10 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2016 Nov 21
Site-specific monoubiquitination downregulates Rab5 by disrupting effector binding and guanine nucleotide conversion. Elife 6 (2017)
Shin D, Na W, Lee JH, Kim G, Baek J, Park SH, Choi CY, Lee S
RgGuinier 2.3 nm
Dmax 8.4 nm

SASDCP6 – Small GTPase Rab5 conjugated with ubiquitin at K165

Monoubiquitinated Rab5 at K165 experimental SAS data
Small GTPase Rab5 conjugated with ubiquitin at K165 Rg histogram
Sample: Monoubiquitinated Rab5 at K165 monomer, 32 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 10 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2016 Nov 21
Site-specific monoubiquitination downregulates Rab5 by disrupting effector binding and guanine nucleotide conversion. Elife 6 (2017)
Shin D, Na W, Lee JH, Kim G, Baek J, Park SH, Choi CY, Lee S
RgGuinier 2.7 nm
Dmax 9.4 nm

SASDCQ2 – 4Ca2+-calmodulin - Xenopus laevis

Calmodulin-1 experimental SAS data
4Ca2+-calmodulin - Xenopus laevis Rg histogram
Sample: Calmodulin-1 monomer, 17 kDa Xenopus laevis protein
Buffer: 25 mM MOPS, 250 mM NaCl, 50 mM KCl, 2 mM TCEP, 0.1% NaN3, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Mar 9
2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update. Acta Crystallogr D Struct Biol 73(Pt 9):710-728 (2017)
Trewhella J, Duff AP, Durand D, Gabel F, Guss JM, Hendrickson WA, Hura GL, Jacques DA, Kirby NM, Kwan AH, Pérez J, Pollack L, Ryan TM, Sali A, Schneidman-Duhovny D, Schwede T, Svergun DI, Sugiyama M, Tainer JA, Vachette P, Westbrook J, Whitten AE
RgGuinier 2.2 nm
Dmax 7.2 nm
VolumePorod 25 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

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

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