Browse by MACROMOLECULE type: protein

SASDRN8 – α/β Hemoglobin (human)

Hemoglobin subunit alphaHemoglobin subunit beta experimental SAS data
Hemoglobin subunit alpha Hemoglobin subunit beta Kratky plot
Sample: Hemoglobin subunit alpha dimer, 31 kDa Homo sapiens protein
Hemoglobin subunit beta dimer, 32 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2021 Oct 7
NSRRC TPS13A standard protein archive
Orion Shih
RgGuinier 2.5 nm
Dmax 9.2 nm
VolumePorod 97 nm3

SASDPL4 – Human MUC2 mucin C-terminal dimer

Human Mucin 2 C-terminal experimental SAS data
DAMMIN model
Sample: Human Mucin 2 C-terminal dimer, 240 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 100 mM NaCl, 10 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2020 Nov 20
The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins Nature Communications 14(1) (2023)
Gallego P, Garcia-Bonete M, Trillo-Muyo S, Recktenwald C, Johansson M, Hansson G
RgGuinier 8.4 nm
Dmax 32.0 nm
VolumePorod 684 nm3

SASDRU7 – Angiotensin-converting enzyme 2/immunoglobulin-Fc chimera protein (Ace2-Fc) at 3.81 mg/ml

Angiotensin-converting enzyme 2 chimera with the Fc region of the immunoglobulin heavy constant gamma 4 experimental SAS data
Angiotensin-converting enzyme 2 chimera with the Fc region of the immunoglobulin heavy constant gamma 4 Kratky plot
Sample: Angiotensin-converting enzyme 2 chimera with the Fc region of the immunoglobulin heavy constant gamma 4 dimer, 217 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2021 Jul 5
Extrinsic stabilization of antiviral ACE2-Fc fusion proteins targeting SARS-CoV-2. Commun Biol 6(1):386 (2023)
Svilenov HL, Delhommel F, Siebenmorgen T, Rührnößl F, Popowicz GM, Reiter A, Sattler M, Brockmeyer C, Buchner J
RgGuinier 5.5 nm
Dmax 18.6 nm
VolumePorod 408 nm3

SASDMR5 – Tn3 family transposase (TnpA WT)

TnpA transposase experimental SAS data
GASBOR model
Sample: TnpA transposase dimer, 234 kDa Bacillus thuringiensis serovar … protein
Buffer: 50 mM HEPES, 200 mM NaCl, 100 mM L-Arg HCL, pH: 7.9
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Nov 2
AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements. Nucleic Acids Res (2023)
Fernandez M, Shkumatov AV, Liu Y, Stulemeijer C, Derclaye S, Efremov RG, Hallet B, Alsteens D
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 480 nm3

SASDS57 – Heterotrimeric membrane protein complex FtsB-FtsL-FtsQ

Cell division protein FtsBCell division protein FtsLCell division protein FtsQ experimental SAS data
DAMMIN model
Sample: Cell division protein FtsB hexamer, 70 kDa Escherichia coli (strain … protein
Cell division protein FtsL hexamer, 82 kDa Escherichia coli (strain … protein
Cell division protein FtsQ hexamer, 189 kDa Escherichia coli (strain … protein
Buffer: 20 mM HEPES pH 7.5, 200 mM NaCl, 0.2% of Cymal-5, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2022 Sep 23
Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome Nature Communications 14(1) (2023)
Nguyen H, Chen X, Parada C, Luo A, Shih O, Jeng U, Huang C, Shih Y, Ma C
RgGuinier 5.3 nm
Dmax 16.5 nm
VolumePorod 421 nm3

SASDQG4 – Rabies virus Nishigahara strain Phosphoprotein Isoform 3 (P3)

Isoform P3 of Phosphoprotein experimental SAS data
Rabies virus Nishigahara strain Phosphoprotein Isoform 3 (P3) Rg histogram
Sample: Isoform P3 of Phosphoprotein dimer, 55 kDa Rabies virus (strain … protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 26
Structural insights into the multifunctionality of rabies virus P3 protein. Proc Natl Acad Sci U S A 120(14):e2217066120 (2023)
Sethi A, Rawlinson SM, Dubey A, Ang CS, Choi YH, Yan F, Okada K, Rozario AM, Brice AM, Ito N, Williamson NA, Hatters DM, Bell TDM, Arthanari H, Moseley GW, Gooley PR
RgGuinier 3.7 nm
Dmax 16.5 nm
VolumePorod 108 nm3

SASDQH4 – Attenuated Nishigahara Phosphoprotein Isoform 3 (Ni-CE P3)

Attenuated derivative P3 of Phosphoprotein experimental SAS data
Attenuated Nishigahara Phosphoprotein Isoform 3 (Ni-CE P3) Rg histogram
Sample: Attenuated derivative P3 of Phosphoprotein dimer, 55 kDa protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 26
Structural insights into the multifunctionality of rabies virus P3 protein. Proc Natl Acad Sci U S A 120(14):e2217066120 (2023)
Sethi A, Rawlinson SM, Dubey A, Ang CS, Choi YH, Yan F, Okada K, Rozario AM, Brice AM, Ito N, Williamson NA, Hatters DM, Bell TDM, Arthanari H, Moseley GW, Gooley PR
RgGuinier 4.0 nm
Dmax 17.5 nm
VolumePorod 127 nm3

SASDQJ4 – N226H Nishigahara Phosphoprotein Isoform 3 (N226H_P3)

Isoform P3 of Phosphoprotein Nish P3 N226H experimental SAS data
N226H Nishigahara Phosphoprotein Isoform 3 (N226H_P3) Rg histogram
Sample: Isoform P3 of Phosphoprotein Nish P3 N226H dimer, 55 kDa protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 26
Structural insights into the multifunctionality of rabies virus P3 protein. Proc Natl Acad Sci U S A 120(14):e2217066120 (2023)
Sethi A, Rawlinson SM, Dubey A, Ang CS, Choi YH, Yan F, Okada K, Rozario AM, Brice AM, Ito N, Williamson NA, Hatters DM, Bell TDM, Arthanari H, Moseley GW, Gooley PR
RgGuinier 4.3 nm
Dmax 19.0 nm
VolumePorod 150 nm3

SASDPV6 – Calmodulin

Calmodulin-1 experimental SAS data
Calmodulin-1 Kratky plot
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 100 mM NaCl, 2 mM CaCl2, 1 mM TCEP, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 Sep 23
Binding by calmodulin is coupled to transient unfolding of the third FF domain of Prp40A. Protein Sci 32(4):e4606 (2023)
Díaz Casas A, Cordoba JJ, Ferrer BJ, Balakrishnan S, Wurm JE, Pastrana-Ríos B, Chazin WJ
RgGuinier 2.2 nm
Dmax 7.0 nm
VolumePorod 38 nm3

SASDPW6 – FF3 domain of pre-mRNA-processing factor 40 homolog A (Prp40A)

Pre-mRNA-processing factor 40 homolog A experimental SAS data
OTHER model
Sample: Pre-mRNA-processing factor 40 homolog A monomer, 9 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 100 mM NaCl, 2 mM CaCl2, 1 mM TCEP, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 Sep 23
Binding by calmodulin is coupled to transient unfolding of the third FF domain of Prp40A. Protein Sci 32(4):e4606 (2023)
Díaz Casas A, Cordoba JJ, Ferrer BJ, Balakrishnan S, Wurm JE, Pastrana-Ríos B, Chazin WJ
RgGuinier 1.6 nm
Dmax 7.2 nm
VolumePorod 13 nm3