Browse by ORGANISM: Homo sapiens (Human)

SASDV47 – Peptide-linked fusion protein of Apoptosis-inducing factor 1 AIF(104-613) point mutant W196A and the N-terminal segment of Mitochondrial intermembrane space import and assembly protein 40 CHCHD4(1-45)

Mitochondrial intermembrane space import and assembly protein 40Apoptosis-inducing factor 1, mitochondrial experimental SAS data
Mitochondrial intermembrane space import and assembly protein 40 Apoptosis-inducing factor 1, mitochondrial Kratky plot
Sample: Mitochondrial intermembrane space import and assembly protein 40 dimer, 12 kDa Homo sapiens protein
Apoptosis-inducing factor 1, mitochondrial dimer, 113 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 28
NADH-bound AIF activates the mitochondrial CHCHD4/MIA40 chaperone by a substrate-mimicry mechanism. EMBO J (2025)
Brosey CA, Shen R, Tainer JA
RgGuinier 3.9 nm
Dmax 12.9 nm
VolumePorod 289 nm3

SASDSK2 – SEC-SAXS data of wild-type estrogen receptor alpha, N-terminal domain (NTD) at pH 7.4

Estrogen receptor experimental SAS data
Estrogen receptor Kratky plot
Sample: Estrogen receptor monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 150 mM NaCl, 0.5 mM EDTA, 0.1 mM PMSF, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jul 21
The sequence–structure–function relationship of intrinsic ERα disorder Nature (2025)
Du Z, Wang H, Luo S, Yun Z, Wu C, Yang W, Buck M, Zheng W, Hansen A, Kao H, Yang S
RgGuinier 3.2 nm
Dmax 14.0 nm
VolumePorod 47 nm3

SASDSE5 – SEC-SAXS data of mutant estrogen receptor alpha (S118A), N-terminal domain (NTD) at pH 7.4

Estrogen receptor (mutant S118A) experimental SAS data
Estrogen receptor (mutant S118A) Kratky plot
Sample: Estrogen receptor (mutant S118A) monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 150 mM NaCl, 0.5 mM EDTA, 0.1 mM PMSF, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jul 21
The sequence–structure–function relationship of intrinsic ERα disorder Nature (2025)
Du Z, Wang H, Luo S, Yun Z, Wu C, Yang W, Buck M, Zheng W, Hansen A, Kao H, Yang S
RgGuinier 3.2 nm
Dmax 15.0 nm
VolumePorod 71 nm3

SASDSF5 – SEC-SAXS data of mutant estrogen receptor alpha (S118D), N-terminal domain (NTD) at pH 7.4

Estrogen receptor (mutant S118D) experimental SAS data
Estrogen receptor (mutant S118D) Kratky plot
Sample: Estrogen receptor (mutant S118D) monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 150 mM NaCl, 0.5 mM EDTA, 0.1 mM PMSF, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jul 21
The sequence–structure–function relationship of intrinsic ERα disorder Nature (2025)
Du Z, Wang H, Luo S, Yun Z, Wu C, Yang W, Buck M, Zheng W, Hansen A, Kao H, Yang S
RgGuinier 3.5 nm
Dmax 16.0 nm
VolumePorod 62 nm3

SASDVC5 – SEC-SAXS data of phosphorylated estrogen receptor alpha (pSer118), N-terminal domain (NTD) at pH 7.4

Estrogen receptor experimental SAS data
Estrogen receptor Kratky plot
Sample: Estrogen receptor monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 50 mM NaCl, 0.05 mM TCEP, pH: 7.4
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source II (NSLS-II) on 2024 Jul 17
The sequence–structure–function relationship of intrinsic ERα disorder Nature (2025)
Du Z, Wang H, Luo S, Yun Z, Wu C, Yang W, Buck M, Zheng W, Hansen A, Kao H, Yang S
RgGuinier 3.6 nm
Dmax 16.0 nm
VolumePorod 70 nm3

SASDUU5 – Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 bound to 3'UTR fragment of ADP-ribosylation factor 1

Double-stranded RNA-binding protein Staufen homolog 1 (Δ1-177)3'UTR fragment of ADP-ribosylation factor 1 experimental SAS data
CORAL model
Sample: Double-stranded RNA-binding protein Staufen homolog 1 (Δ1-177) dimer, 89 kDa Homo sapiens protein
3'UTR fragment of ADP-ribosylation factor 1 monomer, 14 kDa Homo sapiens RNA
Buffer: 50 mM TRIS, 300 mM NaCl, 3.8 mM β-mercaptoethanol, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2020 May 4
A Simple Protocol for Visualization of RNA-Protein Complexes by Atomic Force Microscopy. Curr Protoc 5(1):e70084 (2025)
Tripepi A, Shakoor H, Klapetek P
RgGuinier 4.9 nm
Dmax 13.4 nm
VolumePorod 129 nm3

SASDUV5 – Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) motif bound to 3'UTR fragment of ADP-ribosylation factor 1

3'UTR fragment of ADP-ribosylation factor 1Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) experimental SAS data
CORAL model
Sample: 3'UTR fragment of ADP-ribosylation factor 1 monomer, 14 kDa Homo sapiens RNA
Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) dimer, 81 kDa Homo sapiens protein
Buffer: 50 mM TRIS, 300 mM NaCl, 3.8 mM β-mercaptoethanol, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-2000, CEITEC on 2024 Jan 12
A Simple Protocol for Visualization of RNA-Protein Complexes by Atomic Force Microscopy. Curr Protoc 5(1):e70084 (2025)
Tripepi A, Shakoor H, Klapetek P
RgGuinier 5.5 nm
Dmax 16.1 nm
VolumePorod 139 nm3

SASDSZ5 – DNA binding domain of PALB2 (partner and localizer of BRCA2) in 500 mM NaCl

Partner and localizer of BRCA2 experimental SAS data
DNA binding domain of PALB2 (partner and localizer of BRCA2) in 500 mM NaCl Rg histogram
Sample: Partner and localizer of BRCA2 dimer, 46 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 500 mM NaCl, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Nov 11
The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. iScience 27(12):111259 (2024)
Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S
RgGuinier 5.5 nm
Dmax 25.4 nm
VolumePorod 171 nm3

SASDS26 – DNA binding domain of PALB2 (partner and localizer of BRCA2) in 160 mM NaCl

Partner and localizer of BRCA2 experimental SAS data
DNA binding domain of PALB2 (partner and localizer of BRCA2) in 160 mM NaCl Rg histogram
Sample: Partner and localizer of BRCA2 dimer, 46 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 160 mM NaCl, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Nov 11
The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. iScience 27(12):111259 (2024)
Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S
RgGuinier 4.7 nm
Dmax 21.3 nm
VolumePorod 197 nm3

SASDVQ7 – PABL2 (Partner and localizer of BRCA2) L24A mutant

Partner and localizer of BRCA2 (L24A) experimental SAS data
PABL2 (Partner and localizer of BRCA2) L24A mutant Rg histogram
Sample: Partner and localizer of BRCA2 (L24A) monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 160 mM NaCl, 0.5 mM TCEP pH 7.5, pH: 7.5
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2023 Dec 9
The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. iScience 27(12):111259 (2024)
Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S
RgGuinier 5.2 nm
Dmax 21.6 nm
VolumePorod 127 nm3