|
|
|
|
|
| Sample: |
Gelsolin monomer, 84 kDa Homo sapiens protein
Actin, cytoplasmic 1 18-mer, 751 kDa Gallus gallus protein
|
| Buffer: |
50 mM KCl, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2, 1 mM ATP, 0.1% 2-mercaptoethanol, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Aug 31
|
Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes.
Int J Biol Macromol :134556 (2024)
Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish
|
|
|
|
|
|
|
|
| Sample: |
Gelsolin monomer, 84 kDa Homo sapiens protein
Actin, cytoplasmic 1 18-mer, 751 kDa Gallus gallus protein
|
| Buffer: |
50 mM KCl, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2, 1 mM ATP, 0.1% 2-mercaptoethanol, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Aug 31
|
Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes.
Int J Biol Macromol :134556 (2024)
Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish
|
|
|
|
|
|
|
|
| Sample: |
Gelsolin monomer, 84 kDa Homo sapiens protein
Actin, cytoplasmic 1 18-mer, 751 kDa Gallus gallus protein
|
| Buffer: |
50 mM KCl, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2, 1 mM ATP, 0.1% 2-mercaptoethanol, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Aug 31
|
Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes.
Int J Biol Macromol :134556 (2024)
Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish
|
|
|
|
|
|
|
|
| Sample: |
Gelsolin monomer, 84 kDa Homo sapiens protein
Actin, cytoplasmic 1 monomer, 42 kDa Gallus gallus protein
|
| Buffer: |
2 mM Tris-Cl, pH 8.0, 0.2 mM ATP, 1 mM NaN3, 0.1 mM CaCl2, 0.5 mM DTT, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Aug 31
|
Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes.
Int J Biol Macromol :134556 (2024)
Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish
|
| RgGuinier |
4.7 |
nm |
| Dmax |
25.0 |
nm |
| VolumePorod |
262 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Gelsolin monomer, 84 kDa Homo sapiens protein
Actin, cytoplasmic 1 monomer, 42 kDa Gallus gallus protein
|
| Buffer: |
2 mM Tris-Cl, pH 8.0, 0.2 mM ATP, 1 mM NaN3, 0.1 mM CaCl2, 0.5 mM DTT, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Aug 31
|
Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes.
Int J Biol Macromol :134556 (2024)
Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish
|
| RgGuinier |
5.2 |
nm |
| Dmax |
25.0 |
nm |
| VolumePorod |
266 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/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 |
2.9 |
nm |
| Dmax |
12.0 |
nm |
| VolumePorod |
54 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/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 |
2.9 |
nm |
| Dmax |
12.0 |
nm |
| VolumePorod |
53 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/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
|
|
|
|
|
|
|
|
| Sample: |
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/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
|
|
|
|
|
|
|
|
| Sample: |
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/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
|
|
|