Browse by DISSEMINATION: Published

SASDQ88 – recombinant p123 expressed protein (Gli123)

p123 expressed protein experimental SAS data
DAMMIN model
Sample: P123 expressed protein dimer, 248 kDa Mycoplasma mobile (strain … protein
Buffer: 100 mM ammonium acetate, pH: 6.8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2019 Oct 25
Structure and Function of Gli123 Involved in Mycoplasma mobile Gliding. J Bacteriol :e0034022 (2023)
Matsuike D, Tahara YO, Nonaka T, Wu HN, Hamaguchi T, Kudo H, Hayashi Y, Arai M, Miyata M
RgGuinier 8.2 nm
Dmax 31.6 nm
VolumePorod 436 nm3

SASDQT6 – apo-form of eukaryotic initiation factor 4A1

Eukaryotic initiation factor 4A-I experimental SAS data
Eukaryotic initiation factor 4A-I Kratky plot
Sample: Eukaryotic initiation factor 4A-I monomer, 46 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 100 mM KCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 22
eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation. Nucleic Acids Res (2023)
Schmidt T, Dabrowska A, Waldron JA, Hodge K, Koulouras G, Gabrielsen M, Munro J, Tack DC, Harris G, McGhee E, Scott D, Carlin LM, Huang D, Le Quesne J, Zanivan S, Wilczynska A, Bushell M
RgGuinier 3.1 nm
Dmax 9.8 nm
VolumePorod 80 nm3

SASDQU6 – eukaryotic initiation factor 4A1 bound to 20 nt (AG)10 ssRNA

Eukaryotic initiation factor 4A-I(AG)10-RNA experimental SAS data
Eukaryotic initiation factor 4A-I (AG)10-RNA Kratky plot
Sample: Eukaryotic initiation factor 4A-I monomer, 46 kDa Homo sapiens protein
(AG)10-RNA monomer, 7 kDa synthetic construct RNA
Buffer: 20 mM Hepes, 100 mM KCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Sep 16
eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation. Nucleic Acids Res (2023)
Schmidt T, Dabrowska A, Waldron JA, Hodge K, Koulouras G, Gabrielsen M, Munro J, Tack DC, Harris G, McGhee E, Scott D, Carlin LM, Huang D, Le Quesne J, Zanivan S, Wilczynska A, Bushell M
RgGuinier 2.8 nm
Dmax 10.5 nm
VolumePorod 96 nm3

SASDQV6 – eukaryotic initiation factor 4A1 bound to 20 nt (CAA)6CA ssRNA

Eukaryotic initiation factor 4A-I(CAA)6CA-RNA experimental SAS data
Eukaryotic initiation factor 4A-I (CAA)6CA-RNA Kratky plot
Sample: Eukaryotic initiation factor 4A-I monomer, 46 kDa Homo sapiens protein
(CAA)6CA-RNA monomer, 6 kDa synthetic construct RNA
Buffer: 20 mM Hepes, 100 mM KCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 22
eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation. Nucleic Acids Res (2023)
Schmidt T, Dabrowska A, Waldron JA, Hodge K, Koulouras G, Gabrielsen M, Munro J, Tack DC, Harris G, McGhee E, Scott D, Carlin LM, Huang D, Le Quesne J, Zanivan S, Wilczynska A, Bushell M
RgGuinier 3.1 nm
Dmax 12.8 nm
VolumePorod 89 nm3

SASDQW6 – multimeric eukaryotic initiation factor 4A1 bound to 20 nt (AG)10 ssRNA

(AG)10-RNAEukaryotic initiation factor 4A-I experimental SAS data
(AG)10-RNA Eukaryotic initiation factor 4A-I Kratky plot
Sample: (AG)10-RNA monomer, 7 kDa synthetic construct RNA
Eukaryotic initiation factor 4A-I trimer, 138 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 100 mM KCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Sep 16
eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation. Nucleic Acids Res (2023)
Schmidt T, Dabrowska A, Waldron JA, Hodge K, Koulouras G, Gabrielsen M, Munro J, Tack DC, Harris G, McGhee E, Scott D, Carlin LM, Huang D, Le Quesne J, Zanivan S, Wilczynska A, Bushell M
RgGuinier 3.4 nm
Dmax 13.1 nm
VolumePorod 150 nm3

SASDQX6 – multimeric eukaryotic initiation factor 4A1 bound to 20 nt (AG)10-24bp duplex RNA

Eukaryotic initiation factor 4A-I(AG)10-24bp loading-RNA(AG)10-24bp duplex-RNA experimental SAS data
Eukaryotic initiation factor 4A-I (AG)10-24bp loading-RNA (AG)10-24bp duplex-RNA Kratky plot
Sample: Eukaryotic initiation factor 4A-I trimer, 138 kDa Homo sapiens protein
(AG)10-24bp loading-RNA monomer, 15 kDa synthetic construct RNA
(AG)10-24bp duplex-RNA monomer, 7 kDa synthetic construct RNA
Buffer: 20 mM Hepes, 100 mM KCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Sep 16
eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation. Nucleic Acids Res (2023)
Schmidt T, Dabrowska A, Waldron JA, Hodge K, Koulouras G, Gabrielsen M, Munro J, Tack DC, Harris G, McGhee E, Scott D, Carlin LM, Huang D, Le Quesne J, Zanivan S, Wilczynska A, Bushell M
RgGuinier 4.9 nm
Dmax 16.2 nm
VolumePorod 230 nm3

SASDRS2 – Collagen-like peptide Mannan-binding lectin (MBL) center

Ac-(POG)4-QG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)4-QG-(POG)5-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 2.1 nm
Dmax 8.7 nm
VolumePorod 7 nm3

SASDRT2 – Collagen-like peptide Mannan-binding Lectin (MBL) native

Ac-(POG)4-QG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)4-QG-(POG)5-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 1.7 nm
Dmax 7.1 nm
VolumePorod 4 nm3

SASDRU2 – Collagen-like peptide Mannan-binding lectin (MBL) with EOG sequence

Ac-(POG)5-EOGQGLRG-(POG)3-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)5-EOGQGLRG-(POG)3-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 2.3 nm
Dmax 10.0 nm
VolumePorod 6 nm3

SASDRV2 – Collagen-like peptide Mannan-binding lectin (MBL) 12 triplets

Ac-(POG)5-EPGQGLRG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)5-EPGQGLRG-(POG)5-NH2 trimer, 14 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 12.5 nm
VolumePorod 16 nm3