SASDJK5 – Nucleolysin TIA-1 isoform p40 (TIA-1) bound to TC1 DNA

Nucleolysin TIA-1 isoform p40TC1 experimental SAS data
Nucleolysin TIA-1 isoform p40 TC1 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
TC1 monomer, 3 kDa synthetic construct DNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1. Nucleic Acids Res (2021)
Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA
RgGuinier 3.2 nm
Dmax 15.1 nm
VolumePorod 78 nm3

SASDJL5 – Nucleolysin TIA-1 isoform p40 (TIA-1) bound to UC1 RNA

Nucleolysin TIA-1 isoform p40UC1 experimental SAS data
Nucleolysin TIA-1 isoform p40 UC1 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
UC1 monomer, 3 kDa synthetic construct RNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1. Nucleic Acids Res (2021)
Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA
RgGuinier 3.3 nm
Dmax 14.4 nm
VolumePorod 77 nm3

SASDJM5 – Modified nucleolysin TIA-1 isoform p40 (TIA-1 APO)

Modified Nucleolysin TIA-1 isofrom p40 experimental SAS data
Modified Nucleolysin TIA-1 isofrom p40 Kratky plot
Sample: Modified Nucleolysin TIA-1 isofrom p40 monomer, 42 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 60 mM KCl, 0.5 M arginine-HCl, 1 mM MgCl2, 2 mM DTT, 0.5 mM EDTA, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2020 Jul 7
Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1. Nucleic Acids Res (2021)
Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA
RgGuinier 3.2 nm
Dmax 12.7 nm
VolumePorod 62 nm3

SASDK42 – Chitin-binding protein CbpD (Pseudomonas aeruginosa), ESRF BM29 data

Chitin-binding protein CbpD experimental SAS data
OTHER model
Sample: Chitin-binding protein CbpD monomer, 39 kDa Pseudomonas aeruginosa protein
Buffer: 15 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2020 Oct 1
The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection. Nat Commun 12(1):1230 (2021)
Askarian F, Uchiyama S, Masson H, Sørensen HV, Golten O, Bunæs AC, Mekasha S, Røhr ÅK, Kommedal E, Ludviksen JA, Arntzen MØ, Schmidt B, Zurich RH, van Sorge NM, Eijsink VGH, Krengel U, Mollnes TE, Lew...
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 64131 nm3

SASDJQ5 – Chitin-binding protein CbpD (Pseudomonas aeruginosa) at 24 °C

Chitin-binding protein CbpD experimental SAS data
OTHER model
Sample: Chitin-binding protein CbpD monomer, 39 kDa Pseudomonas aeruginosa protein
Buffer: 15 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar with InCoatec Cu microsource, RECX, University of Oslo on 2019 Jul 19
The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection. Nat Commun 12(1):1230 (2021)
Askarian F, Uchiyama S, Masson H, Sørensen HV, Golten O, Bunæs AC, Mekasha S, Røhr ÅK, Kommedal E, Ludviksen JA, Arntzen MØ, Schmidt B, Zurich RH, van Sorge NM, Eijsink VGH, Krengel U, Mollnes TE, Lew...
RgGuinier 3.3 nm
Dmax 12.1 nm
VolumePorod 50 nm3

SASDJR5 – Chitin-binding protein CbpD (Pseudomonas aeruginosa) at 37°C

Chitin-binding protein CbpD experimental SAS data
Chitin-binding protein CbpD Kratky plot
Sample: Chitin-binding protein CbpD monomer, 39 kDa Pseudomonas aeruginosa protein
Buffer: 15 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar with InCoatec Cu microsource, RECX, University of Oslo on 2019 Aug 14
The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection. Nat Commun 12(1):1230 (2021)
Askarian F, Uchiyama S, Masson H, Sørensen HV, Golten O, Bunæs AC, Mekasha S, Røhr ÅK, Kommedal E, Ludviksen JA, Arntzen MØ, Schmidt B, Zurich RH, van Sorge NM, Eijsink VGH, Krengel U, Mollnes TE, Lew...
RgGuinier 3.5 nm
Dmax 15.0 nm
VolumePorod 63 nm3

SASDK92 – Interferon-activable protein 204 from Mus musculus (Mouse) amino-acids 215-619

Interferon-activable protein 204 experimental SAS data
CHIMERA model
Sample: Interferon-activable protein 204 monomer, 47 kDa Mus musculus protein
Buffer: 20 mM HEPES, 100 mM KCl, pH: 7.4
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2013 Mar 14
Structural mechanism of DNA recognition by the p204 HIN domain. Nucleic Acids Res (2021)
Fan X, Jiang J, Zhao D, Chen F, Ma H, Smith P, Unterholzner L, Xiao TS, Jin T
RgGuinier 3.1 nm
Dmax 9.5 nm
VolumePorod 28 nm3

SASDJL7 – Oxidised fimbrial BcfH protein

Hypothetical exported protein experimental SAS data
CORAL model
Sample: Hypothetical exported protein trimer, 83 kDa Salmonella typhimurium (strain … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 14
Salmonella enterica BcfH is a trimeric thioredoxin-like bifunctional enzyme with both thiol oxidase and disulfide isomerase activities. Antioxid Redox Signal (2021)
Subedi P, Paxman JJ, Wang G, Hor L, Hong Y, Verderosa AD, Whitten AE, Panjikar S, Santos-Martin CF, Martin JL, Totsika M, Heras B
RgGuinier 3.2 nm
Dmax 11.5 nm
VolumePorod 93 nm3

SASDFR7 – Rabbit muscle fructose-bisphosphate aldolase A, K229M mutant

Fructose-bisphosphate aldolase A experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Fructose-bisphosphate aldolase A tetramer, 157 kDa Oryctolagus cuniculus protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, Département de Biochimie, Université de Montréal on 2019 Jun 14
Rabbit muscle fructose-1,6-bisphosphate aldolase K229M mutant
Normand Cyr
RgGuinier 3.6 nm
Dmax 11.8 nm
VolumePorod 213 nm3

SASDJU5 – BIP18SN

BIP18SN experimental SAS data
MODELLER model
Sample: BIP18SN monomer, 80 kDa synthetic construct protein
Buffer: 20 mM Tris 150 mM NaCl 10% glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Nov 28
Self-assembly and regulation of protein cages from pre-organised coiled-coil modules. Nat Commun 12(1):939 (2021)
Lapenta F, Aupič J, Vezzoli M, Strmšek Ž, Da Vela S, Svergun DI, Carazo JM, Melero R, Jerala R
RgGuinier 4.6 nm
Dmax 12.4 nm

5170 hits found.