Browse by MODEL: No model

SASDHC7 – N-terminal engineered, disulfide-containing endo-beta-N-acetylglucosaminidase H at 1052.7 Gy X-ray dose (J/kg)

Endo-beta-N-acetylglucosaminidase H experimental SAS data
Endo-beta-N-acetylglucosaminidase H Kratky plot
Sample: Endo-beta-N-acetylglucosaminidase H dimer, 61 kDa Streptomyces plicatus protein
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Nov 4
SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique PLOS ONE 15(11):e0239702 (2020)
Stachowski T, Snell M, Snell E, Boggon T
RgGuinier 2.8 nm
VolumePorod 60 nm3

SASDHD7 – N-terminal engineered, disulfide-containing endo-beta-N-acetylglucosaminidase H at 1089 Gy X-ray dose (J/kg)

Endo-beta-N-acetylglucosaminidase H experimental SAS data
Endo-beta-N-acetylglucosaminidase H Kratky plot
Sample: Endo-beta-N-acetylglucosaminidase H dimer, 61 kDa Streptomyces plicatus protein
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Nov 4
SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique PLOS ONE 15(11):e0239702 (2020)
Stachowski T, Snell M, Snell E, Boggon T
RgGuinier 2.7 nm
VolumePorod 60 nm3

SASDHE7 – N-terminal engineered, disulfide-containing endo-beta-N-acetylglucosaminidase H at 1125.3 Gy X-ray dose (J/kg)

Endo-beta-N-acetylglucosaminidase H experimental SAS data
Endo-beta-N-acetylglucosaminidase H Kratky plot
Sample: Endo-beta-N-acetylglucosaminidase H dimer, 61 kDa Streptomyces plicatus protein
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Nov 4
SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique PLOS ONE 15(11):e0239702 (2020)
Stachowski T, Snell M, Snell E, Boggon T
RgGuinier 2.7 nm
VolumePorod 61 nm3

SASDHF7 – N-terminal engineered, disulfide-containing endo-beta-N-acetylglucosaminidase H at 1161.6 Gy X-ray dose (J/kg)

Endo-beta-N-acetylglucosaminidase H experimental SAS data
Endo-beta-N-acetylglucosaminidase H Kratky plot
Sample: Endo-beta-N-acetylglucosaminidase H dimer, 61 kDa Streptomyces plicatus protein
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Nov 4
SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique PLOS ONE 15(11):e0239702 (2020)
Stachowski T, Snell M, Snell E, Boggon T
RgGuinier 2.8 nm
VolumePorod 61 nm3

SASDHG7 – N-terminal engineered, disulfide-containing endo-beta-N-acetylglucosaminidase H at 1197.9 Gy X-ray dose (J/kg)

Endo-beta-N-acetylglucosaminidase H experimental SAS data
Endo-beta-N-acetylglucosaminidase H Kratky plot
Sample: Endo-beta-N-acetylglucosaminidase H dimer, 61 kDa Streptomyces plicatus protein
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Nov 4
SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique PLOS ONE 15(11):e0239702 (2020)
Stachowski T, Snell M, Snell E, Boggon T
RgGuinier 2.7 nm
VolumePorod 60 nm3

SASDJT4 – Complex of Candidatus Glomeribacter gigasporarum cyclodipeptide synthase (Cglo-CDPS) with Phe-tRNAPhe

Candidatus Glomeribacter gigasporarum cyclodipeptide synthaseE. coli Phe-tRNAPhe experimental SAS data
Candidatus Glomeribacter gigasporarum cyclodipeptide synthase E. coli Phe-tRNAPhe Kratky plot
Sample: Candidatus Glomeribacter gigasporarum cyclodipeptide synthase monomer, 34 kDa Candidatus Glomeribacter gigasporarum protein
E. coli Phe-tRNAPhe monomer, 25 kDa Escherichia coli RNA
Buffer: 10 mM MOPS pH6.7; 200 mM NaCl, 8 mM MgCl2, pH: 6.7
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Oct 2
Structural basis of the interaction between cyclodipeptide synthases and aminoacylated tRNA substrates. RNA 26(11):1589-1602 (2020)
Bourgeois G, Seguin J, Babin M, Gondry M, Mechulam Y, Schmitt E
RgGuinier 3.3 nm
Dmax 14.0 nm
VolumePorod 77 nm3

SASDHJ8 – ACT domain of the Mycobacterium tuberculosis Rel protein

ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) experimental SAS data
ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) Kratky plot
Sample: ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) dimer, 20 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl, 350 mM NaCl, 5% glycerol, 1 mM DTT, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar, Nanyang Technological University on 2018 Jun 7
Atomic structure of, and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein. FEBS J (2020)
Shin J, Singal B, Manimekalai MSS, Chen MW, Ragunathan P, Grüber G
RgGuinier 1.9 nm
Dmax 6.1 nm
VolumePorod 29 nm3

SASDH74 – Plasmodium falciparum myosin essential light chain, full-length

Myosin essential light chain experimental SAS data
Myosin essential light chain Kratky plot
Sample: Myosin essential light chain monomer, 16 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 2018 Jun 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 23 nm3

SASDH84 – Toxoplasma gondii myosin essential light chain 2

Myosin essential light chain 2 experimental SAS data
Myosin essential light chain 2 Kratky plot
Sample: Myosin essential light chain 2 monomer, 15 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 Apr 8
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 2.1 nm
Dmax 6.7 nm
VolumePorod 27 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