SASDVT4 – Endophilin B1 wild type (0.14 mg/ml)

Endophilin-B1 experimental SAS data
Sample: Endophilin-B1 monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM TCEP, 0.5 mM DTT, pH: 8.1
Experiment: SAXS data collected at BM29, ESRF on 2024 Mar 10
Peripheral membrane protein endophilin B1 probes, perturbs and permeabilizes lipid bilayers Communications Biology 8(1) (2025)
Thorlacius A, Rulev M, Sundberg O, Sundborger-Lunna A
RgGuinier 3.7 nm
Dmax 15.3 nm
VolumePorod 47 nm3

SASDVU4 – Endophilin B1 truncated construction without SH3 domain

Endophilin-B1 (Δ307-360) experimental SAS data
Sample: Endophilin-B1 (Δ307-360) dimer, 68 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM TCEP, 0.5 mM DTT, pH: 8.1
Experiment: SAXS data collected at BM29, ESRF on 2024 Mar 10
Peripheral membrane protein endophilin B1 probes, perturbs and permeabilizes lipid bilayers Communications Biology 8(1) (2025)
Thorlacius A, Rulev M, Sundberg O, Sundborger-Lunna A
RgGuinier 4.6 nm
Dmax 15.2 nm
VolumePorod 149 nm3

SASDW43 – Telomere DNA G-quadruplex (2GKU) at neutral pH

Telomere DNA G-quadruplex Hybrid-1 form experimental SAS data
Telomere DNA G-quadruplex Hybrid-1 form Kratky plot
Sample: Telomere DNA G-quadruplex Hybrid-1 form monomer, 8 kDa synthetic construct DNA
Buffer: 6 mM Na2HPO4, 2 mM NaH2PO4, 1 mM Na2EDTA, 185 mM KCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 11
Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering. Nucleic Acids Res 53(3) (2025)
Monsen RC, Sabo TM, Gray R, Hopkins JB, Chaires JB
RgGuinier 1.2 nm
Dmax 3.8 nm
VolumePorod 8 nm3

SASDW53 – Telomere DNA G-quadruplex (2JSL) at neutral pH

Telomere DNA G-quadruplex Hybrid-2 form experimental SAS data
Telomere DNA G-quadruplex Hybrid-2 form Kratky plot
Sample: Telomere DNA G-quadruplex Hybrid-2 form monomer, 8 kDa synthetic construct DNA
Buffer: 6 mM Na2HPO4, 2 mM NaH2PO4, 1 mM Na2EDTA, 185 mM KCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 11
Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering. Nucleic Acids Res 53(3) (2025)
Monsen RC, Sabo TM, Gray R, Hopkins JB, Chaires JB
RgGuinier 1.2 nm
Dmax 3.8 nm
VolumePorod 8 nm3

SASDW63 – Telomere DNA G-quadruplex (2GKU) at neutral pH with LiCl

Telomere DNA G-quadruplex Hybrid-1 form experimental SAS data
Telomere DNA G-quadruplex Hybrid-1 form Kratky plot
Sample: Telomere DNA G-quadruplex Hybrid-1 form monomer, 8 kDa synthetic construct DNA
Buffer: 6 mM Li2HPO4, 2 mM LiH2PO4, 1 mM EDTA, 185 mM LiCl, pH 7.2, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 11
Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering. Nucleic Acids Res 53(3) (2025)
Monsen RC, Sabo TM, Gray R, Hopkins JB, Chaires JB
RgGuinier 1.2 nm
Dmax 4.3 nm
VolumePorod 7 nm3

SASDW73 – Telomere DNA G-quadruplex (2JSL) at neutral pH with LiCl

Telomere DNA G-quadruplex Hybrid-2 form experimental SAS data
Telomere DNA G-quadruplex Hybrid-2 form Kratky plot
Sample: Telomere DNA G-quadruplex Hybrid-2 form monomer, 8 kDa synthetic construct DNA
Buffer: 6 mM Li2HPO4, 2 mM LiH2PO4, 1 mM EDTA, 185 mM LiCl, pH 7.2, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 12
Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering. Nucleic Acids Res 53(3) (2025)
Monsen RC, Sabo TM, Gray R, Hopkins JB, Chaires JB
RgGuinier 1.3 nm
Dmax 5.1 nm
VolumePorod 8 nm3

SASDW83 – Telomere DNA G-quadruplex (2GKU) at alkaline pH

Telomere DNA G-quadruplex Hybrid-1 form experimental SAS data
Telomere DNA G-quadruplex Hybrid-1 form Kratky plot
Sample: Telomere DNA G-quadruplex Hybrid-1 form monomer, 8 kDa synthetic construct DNA
Buffer: 6 mM Na2HPO4, 2 mM NaH2PO4, 1 mM Na2EDTA, 185 mM KCl, pH 11.5, pH: 11.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 12
Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering. Nucleic Acids Res 53(3) (2025)
Monsen RC, Sabo TM, Gray R, Hopkins JB, Chaires JB
RgGuinier 2.4 nm
Dmax 8.3 nm
VolumePorod 12 nm3

SASDW93 – Telomere DNA G-quadruplex (2JSL) at alkaline pH

Telomere DNA G-quadruplex Hybrid-2 form experimental SAS data
Telomere DNA G-quadruplex Hybrid-2 form Kratky plot
Sample: Telomere DNA G-quadruplex Hybrid-2 form monomer, 8 kDa synthetic construct DNA
Buffer: 6 mM Na2HPO4, 2 mM NaH2PO4, 1 mM Na2EDTA, 185 mM KCl, pH 11.5, pH: 11.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 12
Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering. Nucleic Acids Res 53(3) (2025)
Monsen RC, Sabo TM, Gray R, Hopkins JB, Chaires JB
RgGuinier 2.4 nm
Dmax 8.7 nm
VolumePorod 12 nm3

SASDTU8 – Complement C3* at 1.25 mg/mL (pH 6.0, 200 mM NaCl)

Complement C3 (Δ668-671) experimental SAS data
CORAL model
Sample: Complement C3 (Δ668-671) monomer, 187 kDa Homo sapiens protein
Buffer: 20 mM MES pH 6.0, 200 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Nov 7
Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring. Nat Struct Mol Biol (2025)
Gadeberg TAF, Jørgensen MH, Olesen HG, Lorentzen J, Harwood SL, Almeida AV, Fruergaard MU, Jensen RK, Kanis P, Pedersen H, Tranchant E, Petersen SV, Thøgersen IB, Kragelund BB, Lyons JA, Enghild JJ, A...
RgGuinier 5.4 nm
Dmax 21.8 nm
VolumePorod 357 nm3

SASDVW5 – alpha-amylase AMY3

Alpha-amylase 3, chloroplastic experimental SAS data
BILBOMD model
Sample: Alpha-amylase 3, chloroplastic dimer, 187 kDa Arabidopsis thaliana protein
Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16
The Pseudoenzyme β‐Amylase9 From Arabidopsis Activates α‐Amylase3: A Possible Mechanism to Promote Stress‐Induced Starch Degradation Proteins: Structure, Function, and Bioinformatics (2025)
Berndsen C, Storm A, Sardelli A, Hossain S, Clermont K, McFather L, Connor M, Monroe J
RgGuinier 5.1 nm
Dmax 21.5 nm
VolumePorod 444 nm3

4690 hits found.