Browse by DISSEMINATION: Published

SASDRW2 – [(Pro-Hyp-Gly)10]3

Ac-(POG)10-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)10-NH2 trimer, 12 kDa synthetic construct 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 2.2 nm
Dmax 8.5 nm
VolumePorod 7 nm3

SASDRX2 – [(Pro-Hyp-Gly)13]3

Ac-(POG)13-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)13-NH2 trimer, 15 kDa synthetic construct 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 2.8 nm
Dmax 9.5 nm
VolumePorod 14 nm3

SASDRY2 – [(Pro-Pro-Gly)10]3

[(Pro-Pro-Gly)10]3 experimental SAS data
PYMOL model
Sample: [(Pro-Pro-Gly)10]3 trimer, 8 kDa synthetic construct 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 9.7 nm
VolumePorod 9 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

SASDR23 – [(POG)3-ITGARGLAG-(POG)4]3

Ac-(POG)3-ITGARGLAG-(POG)4-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)3-ITGARGLAG-(POG)4-NH2 trimer, 11 kDa synthetic construct 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 2.2 nm
Dmax 10.0 nm
VolumePorod 9 nm3

SASDQM4 – CRISPR associated Lon protease (CalpL)

SAVED domain-containing protein experimental SAS data
DAMMIF 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 2021 Dec 14
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 3.1 nm
Dmax 10.3 nm
VolumePorod 80 nm3

SASDQN4 – Complex of CRISPR associated Lon protease (CalpL) with a 10 kDa C-terminal fragment of CalpT a putative MazF-like toxin (CalpT10)

SAVED domain-containing proteinUncharacterized protein (putative MazF-like toxin) experimental SAS data
CUSTOM IN-HOUSE model
Sample: SAVED domain-containing protein monomer, 58 kDa Sulfurihydrogenibium sp. (strain … protein
Uncharacterized protein (putative MazF-like toxin) monomer, 9 kDa Sulfurihydrogenibium sp. (strain … protein
Buffer: 20 mM Tris, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Dec 14
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 3.4 nm
Dmax 11.7 nm
VolumePorod 93 nm3

SASDQP4 – CRISPR associated Lon protease (CalpL) in the presence of cyclic oligoadenylate cA4

SAVED domain-containing protein experimental SAS data
DAMMIF 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 3.2 nm
Dmax 10.3 nm
VolumePorod 82 nm3

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

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