SASBDB entries for UniProt ID:

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

UniProt ID: Q6D8U3 (26-924) Ferredoxin protease E83A mutant

UniProt ID: P16972 (53-145) Arabidopsis ferredoxin 2
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)
Grinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, 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

UniProt ID: Q6D8U3 (26-924) Ferredoxin protease E83A mutant

UniProt ID: P16972 (53-145) Arabidopsis ferredoxin 2
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)
Grinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, 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

UniProt ID: Q6D8U3 (26-924) Ferredoxin protease E83A mutant

UniProt ID: P16972 (53-145) Arabidopsis ferredoxin 2
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)
Grinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, 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

UniProt ID: Q6D8U3 (26-924) Ferredoxin protease E83A mutant

UniProt ID: P16972 (53-145) Arabidopsis ferredoxin 2
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)
Grinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, 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

SASDDD7 – Apolipoprotein E2

UniProt ID: P02649 (19-317) Apolipoprotein E2
Apolipoprotein E2 experimental SAS data
Apolipoprotein E2 Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Nov 29
The molecular basis for Apolipoprotein E4 as the major risk factor for late onset Alzheimer's disease. J Mol Biol (2019)
Raulin AC, Kraft L, Al-Hilaly YK, Xue WF, McGeehan JE, Atack JR, Serpell L
RgGuinier 5.6 nm
Dmax 19.5 nm
VolumePorod 400 nm3

SASDDK7 – Disrupted-in-Schizophrenia 1 protein (DISC1 12d2)

UniProt ID: Q9NRI5 (691-836) Disrupted- in-schizophrenia 1 (DISC1 12D2) 691-836
Disrupted- in-schizophrenia 1 (DISC1 12D2) 691-836 experimental SAS data
GASBOR model
Sample: Disrupted- in-schizophrenia 1 (DISC1 12D2) 691-836 monomer, 19 kDa protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 1mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Oct 1
Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein. PLoS One 13(1):e0191162 (2018)
Yerabham ASK, Müller-Schiffmann A, Ziehm T, Stadler A, Köber S, Indurkhya X, Marreiros R, Trossbach SV, Bradshaw NJ, Prikulis I, Willbold D, Weiergräber OH, Korth C
RgGuinier 2.6 nm
Dmax 7.3 nm
VolumePorod 41 nm3

SASDDM7 – Complex of disrupted-in-Schizophrenia 1 protein (DISC1 12D2) and anti-DISC1 single-domain camelid antibody VHH B5

UniProt ID: None (None-None) anti-DISC1 single-domain camelid antibody VHH B5

UniProt ID: Q9NRI5 (691-836) Disrupted- in-schizophrenia 1 (DISC1 12D2) 691-836
anti-DISC1 single-domain camelid antibody VHH B5Disrupted- in-schizophrenia 1 (DISC1 12D2) 691-836 experimental SAS data
DAMMIF model
Sample: Anti-DISC1 single-domain camelid antibody VHH B5 monomer, 14 kDa protein
Disrupted- in-schizophrenia 1 (DISC1 12D2) 691-836 monomer, 19 kDa protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 1mM DTT, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 19
Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein. PLoS One 13(1):e0191162 (2018)
Yerabham ASK, Müller-Schiffmann A, Ziehm T, Stadler A, Köber S, Indurkhya X, Marreiros R, Trossbach SV, Bradshaw NJ, Prikulis I, Willbold D, Weiergräber OH, Korth C
RgGuinier 3.1 nm
Dmax 10.4 nm
VolumePorod 77 nm3

SASDDN7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 May 26
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.3 nm
Dmax 6.7 nm
VolumePorod 88 nm3

SASDDP7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 May 26
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.4 nm
Dmax 6.8 nm
VolumePorod 90 nm3

SASDDQ7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 May 26
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.4 nm
Dmax 7.1 nm
VolumePorod 95 nm3