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SASDQQ4 – CRISPR associated Lon protease (CalpL) asymmetrically dimerizing in the presence of cyclic oligoadenylate cA4

SAVED domain-containing protein experimental SAS data
SASREF MX model
Sample: SAVED domain-containing protein monomer, 58 kDa Sulfurihydrogenibium sp. (strain … protein
Buffer: 20 mM Tris, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Apr 8
Antiviral signalling by a cyclic nucleotide activated CRISPR protease. Nature 614(7946):168-174 (2023)
Rouillon C, Schneberger N, Chi H, Blumenstock K, Da Vela S, Ackermann K, Moecking J, Peter MF, Boenigk W, Seifert R, Bode BE, Schmid-Burgk JL, Svergun D, Geyer M, White MF, Hagelueken G
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 116 nm3

SASDRZ2 – [(Pro-Hyp-Gly)4-POA-(Pro-Hyp-Gly)5]3

Ac-(POG)4-POA-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)4-POA-(POG)5-NH2 trimer, 12 kDa protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.3 nm
Dmax 11.0 nm
VolumePorod 10 nm3

SASDM47 – NAD glycohydrolase (NADase)

NAD glycohydrolase experimental SAS data
BILBOMD model
Sample: NAD glycohydrolase monomer, 47 kDa Streptococcus pyogenes M1 … protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 16
Structural basis underlying the synergism of NADase and SLO during group A Streptococcus infection. Commun Biol 6(1):124 (2023)
Tsai WJ, Lai YH, Shi YA, Hammel M, Duff AP, Whitten AE, Wilde KL, Wu CM, Knott R, Jeng US, Kang CY, Hsu CY, Wu JL, Tsai PJ, Chiang-Ni C, Wu JJ, Lin YS, Liu CC, Senda T, Wang S
RgGuinier 3.0 nm
Dmax 103.0 nm
VolumePorod 66 nm3

SASDM57 – NAD glycohydrolase (NADase)/Streptolysin O (SLO) complex (SAXS with additional contrast variation SANS data)

NAD glycohydrolaseStreptolysin O (T66M) experimental SAS data
BILBOMD model
Sample: NAD glycohydrolase monomer, 47 kDa Streptococcus pyogenes M1 … protein
Streptolysin O (T66M) monomer, 63 kDa Streptococcus pyogenes serotype … protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 16
Structural basis underlying the synergism of NADase and SLO during group A Streptococcus infection. Commun Biol 6(1):124 (2023)
Tsai WJ, Lai YH, Shi YA, Hammel M, Duff AP, Whitten AE, Wilde KL, Wu CM, Knott R, Jeng US, Kang CY, Hsu CY, Wu JL, Tsai PJ, Chiang-Ni C, Wu JJ, Lin YS, Liu CC, Senda T, Wang S
RgGuinier 4.8 nm
Dmax 18.4 nm
VolumePorod 125 nm3

SASDHH7 – Upstream of N-ras, isoform A, CSD 7, 8 and 9 from Drosophila melanogaster

Upstream of N-ras, isoform A experimental SAS data
Upstream of N-ras, isoform A Kratky plot
Sample: Upstream of N-ras, isoform A monomer, 26 kDa Drosophila melanogaster protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 19
Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein. Nucleic Acids Res (2023)
Hollmann NM, Jagtap PKA, Linse JB, Ullmann P, Payr M, Murciano B, Simon B, Hub JS, Hennig J
RgGuinier 2.3 nm
Dmax 9.0 nm
VolumePorod 38 nm3

SASDHL7 – Upstream of N-ras, isoform A, CSD 4 to 9 from Drosophila melanogaster

Upstream of N-ras, isoform A experimental SAS data
Upstream of N-ras, isoform A Kratky plot
Sample: Upstream of N-ras, isoform A monomer, 63 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2019 Sep 30
Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein. Nucleic Acids Res (2023)
Hollmann NM, Jagtap PKA, Linse JB, Ullmann P, Payr M, Murciano B, Simon B, Hub JS, Hennig J
RgGuinier 4.9 nm
Dmax 25.0 nm
VolumePorod 136 nm3

SASDHM7 – Upstream of N-ras, isoform A, CSD 1 to 6 from Drosophila melanogaster

Upstream of N-ras, isoform A experimental SAS data
Upstream of N-ras, isoform A Kratky plot
Sample: Upstream of N-ras, isoform A monomer, 57 kDa Drosophila melanogaster protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Sep 30
Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein. Nucleic Acids Res (2023)
Hollmann NM, Jagtap PKA, Linse JB, Ullmann P, Payr M, Murciano B, Simon B, Hub JS, Hennig J
RgGuinier 4.4 nm
Dmax 20.0 nm
VolumePorod 160 nm3

SASDNN8 – Upstream of N-ras, isoform A, CSD 7, 8 and 9 from Drosophila melanogaster in complex with a poly(A)-15mer RNA

Upstream of N-ras, isoform ApolyA-15mer experimental SAS data
Upstream of N-ras, isoform A polyA-15mer Kratky plot
Sample: Upstream of N-ras, isoform A monomer, 26 kDa Drosophila melanogaster protein
PolyA-15mer monomer, 5 kDa RNA
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 8
Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein. Nucleic Acids Res (2023)
Hollmann NM, Jagtap PKA, Linse JB, Ullmann P, Payr M, Murciano B, Simon B, Hub JS, Hennig J
RgGuinier 2.2 nm
Dmax 7.5 nm
VolumePorod 37 nm3

SASDQG5 – DNA (Zinc finger protein 410 recognition sequence)

DNA (Zinc finger protein 410 recognition sequence) experimental SAS data
DNA (Zinc finger protein 410 recognition sequence) Kratky plot
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 1.8 nm
Dmax 5.8 nm
VolumePorod 16 nm3

SASDQT4 – DNA-binding protein from starved cells: DgrDpsWT in 50 mM MOPS pH 7.0, 230 mM NaCl

DNA protection during starvation, DPS (Ferritin superfamily) experimental SAS data
GASBOR model
Sample: DNA protection during starvation, DPS (Ferritin superfamily) dodecamer, 270 kDa Deinococcus grandis protein
Buffer: 50 mM MOPS-NaOH, 230 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Nov 8
Controlled modulation of the dynamics of the Deinococcus grandis Dps N-terminal tails by divalent metals. Protein Sci :e4567 (2023)
Guerra JPL, Blanchet CE, Vieira BJC, Waerenborgh JC, Jones NC, Hoffmann SV, Pereira AS, Tavares P
RgGuinier 4.5 nm
Dmax 20.0 nm
VolumePorod 454 nm3