SASDHB4 – Trimeric complex of myosin A with myosin light chain (MLC1, residues 66-210) and essential light chain (TgELC1) from Toxoplasma gondii

Myosin light chain TgMLC1, residues 66-210Toxoplasma gondii essential light chain 1Myosin A experimental SAS data
PYMOL model
Sample: Myosin light chain TgMLC1, residues 66-210 monomer, 17 kDa Toxoplasma gondii protein
Toxoplasma gondii essential light chain 1 monomer, 15 kDa Toxoplasma gondii protein
Myosin A monomer, 5 kDa Toxoplasma gondii protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Sep 30
Structural role of essential light chains in the apicomplexan glideosome. Commun Biol 3(1):568 (2020)
Pazicky S, Dhamotharan K, Kaszuba K, Mertens HDT, Gilberger T, Svergun D, Kosinski J, Weininger U, Löw C
RgGuinier 2.7 nm
Dmax 9.5 nm
VolumePorod 50 nm3

SASDHC4 – Trimeric complex of myosin A with myosin light chain (MLC1, residues 70-210) and essential light chain (TgELC1) from Toxoplasma gondii

Toxoplasma gondii essential light chain 1Myosin AToxoplasma gondii myosin light chain, residues 70-210 experimental SAS data
PYMOL model
Sample: Toxoplasma gondii essential light chain 1 monomer, 15 kDa Toxoplasma gondii protein
Myosin A monomer, 5 kDa Toxoplasma gondii protein
Toxoplasma gondii myosin light chain, residues 70-210 monomer, 17 kDa Toxoplasma gondii protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Sep 30
Structural role of essential light chains in the apicomplexan glideosome. Commun Biol 3(1):568 (2020)
Pazicky S, Dhamotharan K, Kaszuba K, Mertens HDT, Gilberger T, Svergun D, Kosinski J, Weininger U, Löw C
RgGuinier 2.5 nm
Dmax 8.2 nm
VolumePorod 47 nm3

SASDHD4 – Trimeric complex of myosin A with myosin light chain (MLC1, residues 66-210) and essential light chain (TgELC2) from Toxoplasma gondii

Myosin essential light chain 2Myosin light chain TgMLC1, residues 66-210Myosin A experimental SAS data
PYMOL model
Sample: Myosin essential light chain 2 monomer, 15 kDa Toxoplasma gondii protein
Myosin light chain TgMLC1, residues 66-210 monomer, 17 kDa Toxoplasma gondii protein
Myosin A monomer, 5 kDa Toxoplasma gondii protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Sep 30
Structural role of essential light chains in the apicomplexan glideosome. Commun Biol 3(1):568 (2020)
Pazicky S, Dhamotharan K, Kaszuba K, Mertens HDT, Gilberger T, Svergun D, Kosinski J, Weininger U, Löw C
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 50 nm3

SASDHE4 – Trimeric complex of myosin A with myosin tail interacting protein (MTIP, residues 60-204) and essential light chain (PfELC) from Plasmodium falciparum

Myosin essential light chainPlasmodium falciparum myosin AMyosin A tail domain interacting protein experimental SAS data
Myosin essential light chain Plasmodium falciparum myosin A Myosin A tail domain interacting protein Kratky plot
Sample: Myosin essential light chain monomer, 16 kDa Plasmodium falciparum protein
Plasmodium falciparum myosin A monomer, 5 kDa Plasmodium falciparum protein
Myosin A tail domain interacting protein monomer, 17 kDa Plasmodium falciparum protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Sep 30
Structural role of essential light chains in the apicomplexan glideosome. Commun Biol 3(1):568 (2020)
Pazicky S, Dhamotharan K, Kaszuba K, Mertens HDT, Gilberger T, Svergun D, Kosinski J, Weininger U, Löw C
RgGuinier 2.7 nm
Dmax 10.7 nm
VolumePorod 51 nm3

SASDJ47 – Polyglutamine protein ataxin-3 (Q13)

Ataxin-3 (polyglutamine protein ataxin-3 (Q13)) experimental SAS data
Polyglutamine protein ataxin-3 (Q13) Rg histogram
Sample: Ataxin-3 (polyglutamine protein ataxin-3 (Q13)) monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate buffer, 2 mM TCEP, 5% glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 24
Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3. Structure (2020)
Sicorello A, Różycki B, Konarev PV, Svergun DI, Pastore A
RgGuinier 4.0 nm
Dmax 14.1 nm
VolumePorod 79 nm3

SASDJ57 – Polyglutamine protein ataxin-3 (Q54)

Ataxin-3 (polyglutamine protein ataxin-3 (Q54)) experimental SAS data
Polyglutamine protein ataxin-3 (Q54) Rg histogram
Sample: Ataxin-3 (polyglutamine protein ataxin-3 (Q54)) monomer, 46 kDa protein
Buffer: 20 mM sodium phosphate buffer, 2 mM TCEP, 5% glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 24
Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3. Structure (2020)
Sicorello A, Różycki B, Konarev PV, Svergun DI, Pastore A
RgGuinier 4.2 nm
Dmax 15.5 nm
VolumePorod 89 nm3

SASDFS7 – Talin-1 head amino acids 1-405(Δ139-168)

Talin-1 (Δ139-168), human experimental SAS data
Talin-1 head amino acids 1-405(Δ139-168) Rg histogram
Sample: Talin-1 (Δ139-168), human monomer, 48 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate, 150mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Sep 24
The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. J Cell Sci 133(19) (2020)
Kukkurainen S, Azizi L, Zhang P, Jacquier MC, Baikoghli M, von Essen M, Tuukkanen A, Laitaoja M, Liu X, Rahikainen R, Orłowski A, Jänis J, Määttä JAE, Varjosalo M, Vattulainen I, Róg T, Svergun D, Che...
RgGuinier 3.3 nm
Dmax 13.3 nm
VolumePorod 77 nm3

SASDFT7 – Talin-1 head amino acids 1-405

Talin-1, human experimental SAS data
Talin-1 head amino acids 1-405 Rg histogram
Sample: Talin-1, human monomer, 51 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Sep 24
The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. J Cell Sci 133(19) (2020)
Kukkurainen S, Azizi L, Zhang P, Jacquier MC, Baikoghli M, von Essen M, Tuukkanen A, Laitaoja M, Liu X, Rahikainen R, Orłowski A, Jänis J, Määttä JAE, Varjosalo M, Vattulainen I, Róg T, Svergun D, Che...
RgGuinier 3.4 nm
Dmax 11.5 nm
VolumePorod 94 nm3

SASDFU7 – Talin-1 head amino acids 1-405(Δ134-170/GAG insert)

Talin-1 (Δ134-170/GAG insert), human experimental SAS data
Talin-1 head amino acids 1-405(Δ134-170/GAG insert) Rg histogram
Sample: Talin-1 (Δ134-170/GAG insert), human monomer, 47 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate, 150mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Sep 24
The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. J Cell Sci 133(19) (2020)
Kukkurainen S, Azizi L, Zhang P, Jacquier MC, Baikoghli M, von Essen M, Tuukkanen A, Laitaoja M, Liu X, Rahikainen R, Orłowski A, Jänis J, Määttä JAE, Varjosalo M, Vattulainen I, Róg T, Svergun D, Che...
RgGuinier 3.0 nm
Dmax 10.2 nm
VolumePorod 71 nm3

SASDGY6 – Salt stress-induced protein at a sample concentration of 5mg/ml

Salt stress-induced protein experimental SAS data
Salt stress-induced protein Kratky plot
Sample: Salt stress-induced protein dimer, 37 kDa Oryza sativa Indica … protein
Buffer: 50 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR - Institute of Microbial Technology (IMTech) on 2017 Mar 6
Structural insights into rice SalTol QTL located SALT protein. Sci Rep 10(1):16589 (2020)
Kaur N, Sagar A, Sharma P, Ashish, Pati PK
RgGuinier 2.5 nm
Dmax 6.7 nm
VolumePorod 56 nm3

4898 hits found.