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43 hits found for Davies

SASDNX3 – Calcium-bound Calmodulin, including structural models

Calmodulin-1 experimental SAS data
Calcium-bound Calmodulin, including structural models Rg histogram
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium. BMC Biol 20(1):176 (2022)
Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
RgGuinier 2.2 nm
Dmax 7.2 nm
VolumePorod 33 nm3

SASDNY3 – Calcium-bound Calmodulin complexed with Calmidazolium

Calmodulin-1Calmidazolium experimental SAS data
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Calmidazolium monomer, 1 kDa
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium. BMC Biol 20(1):176 (2022)
Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
RgGuinier 1.7 nm
Dmax 5.2 nm
VolumePorod 30 nm3

SASDFZ3 – Escherichia coli YjhC

Escherichia coli YjhC experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Escherichia coli YjhC dimer, 86 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1 % (w/v) sodium azide, 5 % (v/v) glycerol, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 12
On the structure and function of Escherichia coli YjhC: an oxidoreductase involved in bacterial sialic acid metabolism. Proteins (2019)
...Davies JS, Dobson RCJ
RgGuinier 3.1 nm
Dmax 10.7 nm
VolumePorod 130 nm3

SASDJ64 – Calcium bound Calmodulin

Calmodulin-1 experimental SAS data
DENSS model
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 4 mM CaCl₂, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Sep 24
A High‐Affinity Calmodulin‐Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells Advanced Science :2003630 (2021)
Voegele A, Sadi M, O'Brien D, Gehan P, Raoux‐Barbot D, Davi M, Hoos S, Brûlé S, Raynal B, Weber P, Mechaly A, Haouz A, Rodriguez N, Vachette P, Durand D, Brier S, Ladant D, Chenal A
RgGuinier 2.2 nm
Dmax 7.3 nm
VolumePorod 27 nm3

SASDJ74 – P454 peptide from B.pertussis CyaA toxin complexed with calmodulin

Calmodulin-1Bifunctional hemolysin/adenylate cyclase experimental SAS data
DENSS model
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Bifunctional hemolysin/adenylate cyclase monomer, 3 kDa Bordetella pertussis protein
Buffer: 20 mM HEPES, 150 mM NaCl, 4 mM CaCl₂, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Sep 24
A High‐Affinity Calmodulin‐Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells Advanced Science :2003630 (2021)
Voegele A, Sadi M, O'Brien D, Gehan P, Raoux‐Barbot D, Davi M, Hoos S, Brûlé S, Raynal B, Weber P, Mechaly A, Haouz A, Rodriguez N, Vachette P, Durand D, Brier S, Ladant D, Chenal A
RgGuinier 2.0 nm
Dmax 7.0 nm
VolumePorod 28 nm3

SASDFM5 – Mutant 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, H110A tetramer, at pH 8.5

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, 159 kDa Pseudomonas fluorescens protein
Buffer: 50 mM Tris, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jul 15
Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity. J Biol Chem 294(30):11609-11621 (2019)
Yang Y, Davis I, Matsui T, Rubalcava I, Liu A
RgGuinier 5.2 nm
Dmax 19.0 nm
VolumePorod 238 nm3

SASDFN5 – Wild type 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, ACMSD tetramer, at pH 7.0

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, 159 kDa Pseudomonas fluorescens protein
Buffer: 25 mM HEPES, 5 mM DTT, pH: 7
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jan 10
Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity. J Biol Chem 294(30):11609-11621 (2019)
Yang Y, Davis I, Matsui T, Rubalcava I, Liu A
RgGuinier 4.7 nm
Dmax 17.5 nm
VolumePorod 195 nm3

SASDNN5 – Meiosis protein TEX12 (Testis-expressed protein 12) – wild-type

Testis-expressed protein 12 experimental SAS data
DAMMIF model
Sample: Testis-expressed protein 12 dimer, 18 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jan 10
Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip Communications Biology 5(1) (2022)
...Davies O
RgGuinier 2.1 nm
Dmax 6.6 nm
VolumePorod 27 nm3

SASDNP5 – Meiosis protein TEX12 (Testis-expressed protein 12) – delta Ctip

Testis-expressed protein 12 experimental SAS data
DAMMIF model
Sample: Testis-expressed protein 12 tetramer, 32 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jan 10
Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip Communications Biology 5(1) (2022)
...Davies O
RgGuinier 3.0 nm
Dmax 11.0 nm
VolumePorod 44 nm3

SASDNQ5 – Meiosis protein TEX12 (Testis-expressed protein 12) – L110E, F114E, I117E, L121E mutant

Testis-expressed protein 12 (L110E, F114E, I117E, L121E) experimental SAS data
DAMMIF model
Sample: Testis-expressed protein 12 (L110E, F114E, I117E, L121E) tetramer, 36 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Sep 15
Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip Communications Biology 5(1) (2022)
...Davies O
RgGuinier 3.3 nm
Dmax 12.9 nm
VolumePorod 59 nm3

SASDNR5 – Meiosis protein TEX12 (Testis-expressed protein 12) – F102A, F109E, V116A mutant

Testis-expressed protein 12 (F102A, F109E, V116A) experimental SAS data
DAMMIF model
Sample: Testis-expressed protein 12 (F102A, F109E, V116A) tetramer, 36 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Nov 27
Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip Communications Biology 5(1) (2022)
...Davies O
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 48 nm3

SASDNS5 – Meiosis protein TEX12 (Testis-expressed protein 12) – F109E mutant

Testis-expressed protein 12 (F109E) experimental SAS data
DAMMIF model
Sample: Testis-expressed protein 12 (F109E) dimer, 18 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Sep 13
Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip Communications Biology 5(1) (2022)
...Davies O
RgGuinier 2.3 nm
Dmax 7.5 nm
VolumePorod 30 nm3

SASDEA6 – Staphylococcus aureus N-acetylglucosamine-6-phosphate deacetylase dimer

N-acetylglucosamine-6-phosphate deacetylase experimental SAS data
PYMOL model
Sample: N-acetylglucosamine-6-phosphate deacetylase dimer, 86 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris-HCl 150 mM NaCl, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Apr 26
Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus. FEBS Lett (2018)
Davies JS, Coombes D, Horne CR, Pearce FG, Friemann R, North RA, Dobson RCJ
RgGuinier 3.2 nm
Dmax 10.1 nm
VolumePorod 107 nm3

SASDEB6 – Staphylococcus aureus glucosamine-6-phosphate deaminase

Glucosamine-6-phosphate deaminase experimental SAS data
PYMOL model
Sample: Glucosamine-6-phosphate deaminase dimer, 57 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris-HCl 150 mM NaCl, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Apr 26
Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus. FEBS Lett (2018)
Davies JS, Coombes D, Horne CR, Pearce FG, Friemann R, North RA, Dobson RCJ
RgGuinier 2.7 nm
Dmax 8.9 nm
VolumePorod 84 nm3

SASDDQ6 – The ferredoxin protease, FusC

Ferredoxin Protease experimental SAS data
Ferredoxin Protease Kratky plot
Sample: Ferredoxin Protease monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 6
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 12.8 nm
VolumePorod 152 nm3

SASDDR6 – The ferredoxin protease, FusC, E83A mutant

Ferredoxin protease E83A mutant experimental SAS data
Ferredoxin protease E83A mutant Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Buffer: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 6
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 12.7 nm
VolumePorod 152 nm3

SASDDS6 – The ferredoxin protease, FusC, with Arabidopsis ferredoxin (co-SEC-SAXS)

Ferredoxin ProteaseArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin Protease Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin Protease monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 6
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 13.2 nm
VolumePorod 156 nm3

SASDDT6 – The ferredoxin protease, FusC, E83A mutant with Arabidopsis ferredoxin (co-SEC-SAXS)

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 6
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.6 nm
Dmax 12.7 nm
VolumePorod 161 nm3

SASDDU6 – The ferredoxin protease, FusC, E83A mutant

Ferredoxin protease E83A mutant experimental SAS data
Ferredoxin protease E83A mutant Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 13.8 nm
VolumePorod 152 nm3

SASDDV6 – The ferredoxin protease, FusC, E83A mutant + 3 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 13.8 nm
VolumePorod 150 nm3

SASDDW6 – The ferredoxin protease, FusC, E83A mutant + 5 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 13.7 nm
VolumePorod 148 nm3

SASDDX6 – The ferredoxin protease, FusC, E83A mutant + 10 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 13.6 nm
VolumePorod 149 nm3

SASDDY6 – The ferredoxin protease, FusC, E83A mutant + 20 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 13.6 nm
VolumePorod 155 nm3

SASDDZ6 – The ferredoxin protease, FusC, E83A mutant + 30 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 14.0 nm
VolumePorod 156 nm3

SASDD27 – The ferredoxin protease, FusC, E83A mutant + 50 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 160 nm3

SASDD37 – The ferredoxin protease, FusC, E83A mutant + 70 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 14.0 nm
VolumePorod 165 nm3

SASDD47 – The ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 13.7 nm
VolumePorod 177 nm3

SASDD57 – The ferredoxin protease, FusC, E83A mutant + 150 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.8 nm
Dmax 14.2 nm
VolumePorod 178 nm3

SASDD67 – The ferredoxin protease, FusC, E83A mutant + 200 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 14.0 nm
VolumePorod 175 nm3

SASDD77 – The ferredoxin protease, FusC, E83A mutant + 300 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
...Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
RgGuinier 3.7 nm
Dmax 14.0 nm
VolumePorod 180 nm3

SASDH99 – Meiotic localizer of BRCA2 bound to BRME1 - MEILB2a1+2-BRME1 2:2 complex

BRME1Meiotic localizer of BRCA2 experimental SAS data
DAMMIF model
Sample: BRME1 dimer, 23 kDa Mus musculus protein
Meiotic localizer of BRCA2 dimer, 26 kDa Mus musculus protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Oct 7
The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs the mitotic BRCA2-RAD51 function in cancer cells Nature Communications 11(1) (2020)
...Davies O, Shibuya H
RgGuinier 5.0 nm
Dmax 19.0 nm
VolumePorod 104 nm3

SASDHA9 – Meiotic localizer of BRCA2 - MEILB2a1+2 dimer

Meiotic localizer of BRCA2 experimental SAS data
DAMMIF model
Sample: Meiotic localizer of BRCA2 dimer, 26 kDa Mus musculus protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Oct 7
The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs the mitotic BRCA2-RAD51 function in cancer cells Nature Communications 11(1) (2020)
...Davies O, Shibuya H
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 88 nm3

SASDHB9 – Meiotic localizer of BRCA2 - MEILB2a1+2 octamer

Meiotic localizer of BRCA2 experimental SAS data
DAMMIF model
Sample: Meiotic localizer of BRCA2 octamer, 102 kDa Mus musculus protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Oct 7
The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs the mitotic BRCA2-RAD51 function in cancer cells Nature Communications 11(1) (2020)
...Davies O, Shibuya H
RgGuinier 5.7 nm
Dmax 20.0 nm
VolumePorod 368 nm3

SASDHC9 – Meiotic localizer of BRCA2 - MEILB1a2 monomer

Meiotic localizer of BRCA2 experimental SAS data
DAMMIF model
Sample: Meiotic localizer of BRCA2 monomer, 9 kDa Mus musculus protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Oct 7
The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs the mitotic BRCA2-RAD51 function in cancer cells Nature Communications 11(1) (2020)
...Davies O, Shibuya H
RgGuinier 3.0 nm
Dmax 11.0 nm
VolumePorod 43 nm3

SASDCK9 – Catalytic domain (AC) of B. Pertussis Adenylate Cyclase Toxin (CyaA)

Bifunctional hemolysin/adenylate cyclase experimental SAS data
ALLOSMOD model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 39 kDa Bordetella pertussis protein
Buffer: 20 mM Hepes, 150 mM NaCl, 4 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Jun 19
Calmodulin fishing with a structurally disordered bait triggers CyaA catalysis. PLoS Biol 15(12):e2004486 (2017)
O'Brien DP, Durand D, Voegele A, Hourdel V, Davi M, Chamot-Rooke J, Vachette P, Brier S, Ladant D, Chenal A
RgGuinier 2.6 nm
Dmax 9.1 nm
VolumePorod 60 nm3

SASDCL9 – Catalytic domain (AC) of B. Pertussis Adenylate Cyclase Toxin (CyaA) in complex with calmodulin

Bifunctional hemolysin/adenylate cyclaseCalmodulin experimental SAS data
BUNCH model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 39 kDa Bordetella pertussis protein
Calmodulin monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 150 mM NaCl, 4 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Jun 19
Calmodulin fishing with a structurally disordered bait triggers CyaA catalysis. PLoS Biol 15(12):e2004486 (2017)
O'Brien DP, Durand D, Voegele A, Hourdel V, Davi M, Chamot-Rooke J, Vachette P, Brier S, Ladant D, Chenal A
RgGuinier 2.9 nm
Dmax 9.8 nm
VolumePorod 78 nm3

SASDJF5 – SUN domain of SUN1 harbouring mutation I673E - monomer

SUN domain-containing protein 1, I673E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: SUN domain-containing protein 1, I673E monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Jul 29
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
...Davies OR
RgGuinier 2.1 nm
Dmax 8.2 nm
VolumePorod 42 nm3

SASDL56 – 14-3-3 zeta truncated at C-terminus

14-3-3 protein zeta/delta experimental SAS data
14-3-3 protein zeta/delta Kratky plot
Sample: 14-3-3 protein zeta/delta dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Oct 13
A structural study of the cytoplasmic chaperone effect of 14-3-3 proteins on Ataxin-1. J Mol Biol :167174 (2021)
Leysen S, Jane Burnley R, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Yahya Zoghbi H, Ottmann C, Martin Davis J
RgGuinier 2.8 nm
Dmax 7.9 nm

SASDLT3 – Ataxin-1 AXH-C

Ataxin-1 experimental SAS data
Ataxin-1 AXH-C Rg histogram
Sample: Ataxin-1 dimer, 55 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Oct 13
A structural study of the cytoplasmic chaperone effect of 14-3-3 proteins on Ataxin-1. J Mol Biol :167174 (2021)
Leysen S, Jane Burnley R, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Yahya Zoghbi H, Ottmann C, Martin Davis J
RgGuinier 4.3 nm
Dmax 14.6 nm
VolumePorod 90 nm3

SASDJC5 – LINC complex between the SUN domain of SUN1 and KASH domain of Nesprin-4 - SUN1-KASH4 6:6 complex

SUN domain-containing protein 1Nesprin-4 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: SUN domain-containing protein 1 hexamer, 135 kDa Homo sapiens protein
Nesprin-4 hexamer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 21
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
...Davies OR
RgGuinier 4.0 nm
Dmax 13.5 nm
VolumePorod 240 nm3

SASDJD5 – LINC complex between the SUN domain of SUN1 and KASH domain of KASH5 - SUN1-KASH5 6:6 complex

SUN domain-containing protein 1Protein KASH5 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: SUN domain-containing protein 1 hexamer, 135 kDa Homo sapiens protein
Protein KASH5 hexamer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Dec 17
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
...Davies OR
RgGuinier 3.8 nm
Dmax 13.5 nm
VolumePorod 244 nm3

SASDL46 – 14-3-3zeta AXH-C complex

14-3-3 protein zeta/deltaAtaxin-1 AXH-C experimental SAS data
MULTIFOXS model
Sample: 14-3-3 protein zeta/delta dimer, 53 kDa Homo sapiens protein
Ataxin-1 AXH-C dimer, 55 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Oct 13
A structural study of the cytoplasmic chaperone effect of 14-3-3 proteins on Ataxin-1. J Mol Biol :167174 (2021)
Leysen S, Jane Burnley R, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Yahya Zoghbi H, Ottmann C, Martin Davis J
RgGuinier 4.8 nm
Dmax 19.8 nm

SASDJE5 – LINC complex between the SUN domain of SUN1 and KASH domain of Nesprin-1 - SUN1-KASH1 6:6 complex

SUN domain-containing protein 1Nesprin-1 experimental SAS data
CORAL model
Sample: SUN domain-containing protein 1 hexamer, 135 kDa Homo sapiens protein
Nesprin-1 hexamer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Dec 17
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
...Davies OR
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 254 nm3