Browse by MACROMOLECULE type: protein

SASDTM8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 50 MPa

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.0 nm

SASDTN8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 100 MPa

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.2 nm

SASDTP8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 150 MPa

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 2.9 nm

SASDTQ8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 200 MPa

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.1 nm

SASDTR8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 250 MPa

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.2 nm

SASDR98 – The BTB domain (wild-type) of the zinc finger and BTB domain-containing protein 8A.1-A (ZBTB8a) from Xenopus laevis

Zinc finger and BTB domain-containing protein 8A.1-A experimental SAS data
Zinc finger and BTB domain-containing protein 8A.1-A Kratky plot
Sample: Zinc finger and BTB domain-containing protein 8A.1-A dimer, 35 kDa Xenopus laevis protein
Buffer: 20 mM Hepes, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2022 Dec 4
Dynamic BTB-domain filaments promote clustering of ZBTB proteins. Mol Cell 84(13):2490-2510.e9 (2024)
Mance L, Bigot N, Zhamungui Sánchez E, Coste F, Martín-González N, Zentout S, Biliškov M, Pukało Z, Mishra A, Chapuis C, Arteni AA, Lateur A, Goffinont S, Gaudon V, Talhaoui I, Casuso I, Beaufour M, Garnier N, Artzner F, Cadene M, Huet S, Castaing B, Suskiewicz MJ
RgGuinier 22.3 nm
Dmax 99.6 nm

SASDRA8 – The BTB domain (S103R mutant) of the zinc finger and BTB domain-containing protein 8A.1-A (ZBTB8a) from Xenopus laevis

Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant) experimental SAS data
Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant) Kratky plot
Sample: Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant) dimer, 35 kDa Xenopus laevis protein
Buffer: 20 mM Hepes, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2022 Dec 4
Dynamic BTB-domain filaments promote clustering of ZBTB proteins. Mol Cell 84(13):2490-2510.e9 (2024)
Mance L, Bigot N, Zhamungui Sánchez E, Coste F, Martín-González N, Zentout S, Biliškov M, Pukało Z, Mishra A, Chapuis C, Arteni AA, Lateur A, Goffinont S, Gaudon V, Talhaoui I, Casuso I, Beaufour M, Garnier N, Artzner F, Cadene M, Huet S, Castaing B, Suskiewicz MJ
RgGuinier 3.3 nm
Dmax 12.8 nm
VolumePorod 60 nm3

SASDUA4 – Ribonuclease A Updated Consensus SAXS Data

Ribonuclease pancreatic experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ribonuclease pancreatic monomer, 14 kDa Bos taurus protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.5
Experiment: SANS data collected at (Consensus SAS), Multi-facility, Multiple countries on 2024 Feb 4
Benchmarking predictive methods for small-angle X-ray scattering from atomic coordinates of proteins using maximum likelihood consensus data IUCrJ 11(5) (2024)
Trewhella J, Vachette P, Larsen A
RgGuinier 1.5 nm
Dmax 5.0 nm

SASDUB4 – Urate Oxidase Updated Consensus SAXS Data

Uricase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Uricase tetramer, 136 kDa Aspergillus flavus protein
Buffer: 100 mM Tris, 150 mM NaCl, pH: 8
Experiment: SANS data collected at (Consensus SAS), Multi-facility, Multiple countries on 2024 Feb 4
Benchmarking predictive methods for small-angle X-ray scattering from atomic coordinates of proteins using maximum likelihood consensus data IUCrJ 11(5) (2024)
Trewhella J, Vachette P, Larsen A
RgGuinier 3.2 nm
Dmax 9.3 nm

SASDUC4 – Xylose Isomerase Updated Consensus SAXS Data

Xylose isomerase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Xylose isomerase tetramer, 173 kDa Streptomyces rubiginosus protein
Buffer: 50 mM Tris, 100 mM NaCl, 1 mM MgCl2, pH: 7.5
Experiment: SANS data collected at (Consensus SAS), Multi-facility, Multiple countries on 2024 Feb 4
Benchmarking predictive methods for small-angle X-ray scattering from atomic coordinates of proteins using maximum likelihood consensus data IUCrJ 11(5) (2024)
Trewhella J, Vachette P, Larsen A
RgGuinier 3.3 nm
Dmax 10.1 nm