SASBDB entries for UniProt ID:

SASDT98 – UP1 domain of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 150 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1

Heterogeneous nuclear ribonucleoprotein A1 experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 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 2.4 nm
Dmax 10.0 nm
VolumePorod 29 nm3

SASDTA8 – UP1 domain of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 200 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1

Heterogeneous nuclear ribonucleoprotein A1 experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 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 2.4 nm
Dmax 9.5 nm
VolumePorod 28 nm3

SASDTB8 – UP1 domain of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 250 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1

Heterogeneous nuclear ribonucleoprotein A1 experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 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 2.4 nm
Dmax 9.5 nm
VolumePorod 29 nm3

SASDTC8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut); SEC-SAXS, July 2022)

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 34 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12-ID-B, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Jul 7
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 3.4 nm
Dmax 14.0 nm
VolumePorod 57 nm3

SASDTD8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut); SEC-SAXS, Sept 2022)

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 34 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12-ID-B, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Sep 27
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 3.7 nm
Dmax 14.0 nm
VolumePorod 58 nm3

SASDTE8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut)) at 0.1 MPa

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 34 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 3.6 nm
Dmax 20.0 nm
VolumePorod 98 nm3

SASDTF8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut)) at 50 MPa

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 34 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 3.7 nm
Dmax 23.0 nm
VolumePorod 104 nm3

SASDTG8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut)) at 100 MPa

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 34 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 3.6 nm
Dmax 23.0 nm
VolumePorod 94 nm3

SASDTH8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut)) at 150 MPa

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 34 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 3.6 nm
Dmax 23.0 nm
VolumePorod 109 nm3

SASDTJ8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut)) at 200 MPa

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 34 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 3.7 nm