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35 hits found for Song

SASDK82 – Full-length nonstructural protein 2 (nsP2) of Chikungunya virus (CHIKV)

NsP2 protein experimental SAS data
CORAL model
Sample: NsP2 protein monomer, 90 kDa Chikungunya virus protein
Buffer: 20 mM Hepes pH 7.4, 150 mM NaCl, 1 mM DTT, 5% glycerol, pH: 7.4
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2019 Aug 10
Inter-domain Flexibility of Chikungunya Virus nsP2 Helicase-Protease Differentially Influences Viral RNA Replication and Infectivity. J Virol (2020)
Law YS, Wang S, Tan YB, Shih O, Utt A, Goh WY, Lian BJ, Chen MW, Jeng US, Merits A, Luo D
RgGuinier 3.9 nm
Dmax 12.0 nm
VolumePorod 134 nm3

SASDLT2 – 6D11 IgG monoclonal antibody

Anti-prion protein monoclonal IgG2a 6D11 experimental SAS data
CORAL model
Sample: Anti-prion protein monoclonal IgG2a 6D11 monomer, 145 kDa Mus musculus protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 15
Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies. Sci Adv 7(48):eabj1826 (2021)
...Song F, Schwarz A, Da Vela S, Massignan T, Jung S, Correia A, Schmitz M, Puig B, Hornemann S, Zerr I, Tatzelt J, Biasini E, Saftig P, Schweizer M, Svergun D, Amin L, Mazzola F, Varani L, Thapa S, Gilc...
RgGuinier 5.1 nm
Dmax 17.4 nm
VolumePorod 330 nm3

SASDLU2 – 2:1 complex between anti prion protein monoclonal IgG 6D11 and recombinant murine prion protein

Major prion proteinAnti-prion protein monoclonal IgG2a 6D11 experimental SAS data
OTHER model
Sample: Major prion protein monomer, 23 kDa Mus musculus protein
Anti-prion protein monoclonal IgG2a 6D11 monomer, 145 kDa Mus musculus protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 15
Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies. Sci Adv 7(48):eabj1826 (2021)
...Song F, Schwarz A, Da Vela S, Massignan T, Jung S, Correia A, Schmitz M, Puig B, Hornemann S, Zerr I, Tatzelt J, Biasini E, Saftig P, Schweizer M, Svergun D, Amin L, Mazzola F, Varani L, Thapa S, Gilc...
RgGuinier 8.1 nm
Dmax 24.8 nm
VolumePorod 710 nm3

SASDH45 – Histone Deacetylase 1 (HDAC1) and Lysine-specific Demethylase 1 (LSD1) in the complex with CoREST

Histone deacetylase 1Lysine-specific histone demethylase 1AREST corepressor 1 experimental SAS data
DAMFILT model
Sample: Histone deacetylase 1 monomer, 55 kDa Homo sapiens protein
Lysine-specific histone demethylase 1A monomer, 93 kDa Homo sapiens protein
REST corepressor 1 monomer, 46 kDa Homo sapiens protein
Buffer: 25 mM Tris/Cl, 50 mM potassium acetate and 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2015 Jan 23
Mechanism of Crosstalk between the LSD1 Demethylase and HDAC1 Deacetylase in the CoREST Complex. Cell Rep 30(8):2699-2711.e8 (2020)
Song Y, Dagil L, Fairall L, Robertson N, Wu M, Ragan TJ, Savva CG, Saleh A, Morone N, Kunze MBA, Jamieson AG, Cole PA, Hansen DF, Schwabe JWR
RgGuinier 6.0 nm
Dmax 15.8 nm
VolumePorod 437 nm3

SASDJX5 – Solution Scattering of Zeitlupe G46S:G80R

Adagio protein 1 (Zeitlupe G46S:G80R) experimental SAS data
DAMMIN model
Sample: Adagio protein 1 (Zeitlupe G46S:G80R) dimer, 37 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM NaCl, 2 mM TCEP, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Nov 2
Steric and Electronic Interactions at Gln154 in ZEITLUPE Induce Reorganization of the LOV Domain Dimer Interface. Biochemistry (2020)
...Song YH, Blumenfeld A, Karki N, Imaizumi T, Zoltowski BD
RgGuinier 2.2 nm
Dmax 8.4 nm
VolumePorod 41 nm3

SASDD46 – Artificially designed de novo protein esPN-Block (HL4) heterocomplex, e1s2 (HL4)

extender PN-Block (HL4)stopper PN-Block (WA20) experimental SAS data
DAMMIN model
Sample: extender PN-Block (HL4) monomer, 27 kDa de novo protein protein
stopper PN-Block (WA20) dimer, 25 kDa de novo protein protein
Buffer: 20 mM HEPES, 100 mM NaCl, 200 mM ArgHCl, 10% glycerol, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2014 Dec 19
Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks. ACS Synth Biol 7(5):1381-1394 (2018)
...Song C, Murata K, Arai R
RgGuinier 3.6 nm
Dmax 15.0 nm

SASDD56 – Artificially designed de novo protein esPN-Block (FL4) heterocomplex, e1s2 (FL4)

stopper PN-Block (WA20)extender PN-Block (FL4) experimental SAS data
DAMMIN model
Sample: stopper PN-Block (WA20) dimer, 25 kDa de novo protein protein
extender PN-Block (FL4) monomer, 27 kDa de novo protein protein
Buffer: 20 mM HEPES, 100 mM NaCl, 200 mM ArgHCl, 10% glycerol, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2014 Dec 19
Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks. ACS Synth Biol 7(5):1381-1394 (2018)
...Song C, Murata K, Arai R
RgGuinier 3.3 nm
Dmax 12.0 nm

SASDK86 – wild-type TRIM72 (Tripartite motif-containing protein 72)

Tripartite motif-containing protein 72 experimental SAS data
DAMMIN model
Sample: Tripartite motif-containing protein 72 dimer, 105 kDa Mus musculus protein
Buffer: 25 mM Tris-HCl, pH 8.0, 300 mM NaCl, 1 mM TCEP, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2019 Dec 7
Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane. Nat Struct Mol Biol (2023)
...Song JH, Jang SH, Jeong H, Kim BH, Ko YG, Park ZY, Lee KE, Hyun J, Song HK
RgGuinier 6.9 nm
Dmax 24.0 nm
VolumePorod 384 nm3

SASDK96 – tripartite motif-containing protein 72 (TRIM72) lacking the zinc finger RING domain (ΔRING)

Tripartite motif-containing protein 72 experimental SAS data
OTHER model
Sample: Tripartite motif-containing protein 72 dimer, 88 kDa Mus musculus protein
Buffer: 25 mM Tris-HCl, pH 8.0, 300 mM NaCl, 1 mM TCEP, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2019 Dec 7
Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane. Nat Struct Mol Biol (2023)
...Song JH, Jang SH, Jeong H, Kim BH, Ko YG, Park ZY, Lee KE, Hyun J, Song HK
RgGuinier 5.1 nm
Dmax 18.7 nm
VolumePorod 142 nm3

SASDFA6 – Proteolytic fragment of phage flagella binding tail protein YSD1_29 (amino acids 373-1296)

Flagella binding tail protein experimental SAS data
DAMMIF model
Sample: Flagella binding tail protein monomer, 103 kDa Salmonella virus Chi 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 4
The flagellotropic bacteriophage YSD1 targets Salmonella Typhi with a Chi-like protein tail fibre. Mol Microbiol (2019)
...Song J, Schreiber F, Choudhary J, Clare S, Coulibaly F, Strugnell RA, Dougan G, Lithgow T
RgGuinier 5.6 nm
Dmax 27.4 nm
VolumePorod 155 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)
...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 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)
...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 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)
...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 13.2 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)
...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 3.6 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)
...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 13.8 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)
...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 13.8 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)
...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 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)
...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 13.6 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)
...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 13.6 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)
...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 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)
...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 14.0 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)
...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 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)
...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

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)
...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

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)
...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

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)
...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

SASDFD7 – Pseudomonas putida CBB5 NdmAB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 127 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
...Song HK
RgGuinier 4.5 nm
Dmax 12.3 nm

SASDFE7 – Pseudomonas putida CBB5 mCherry-NdmA/NdmB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 207 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
...Song HK
RgGuinier 5.4 nm
Dmax 13.8 nm

SASDFF7 – Pseudomonas putida CBB5 NdmA hexamer

Methylxanthine N1-demethylase NdmA experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA hexamer, 254 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
...Song HK
RgGuinier 4.2 nm
Dmax 11.0 nm

SASDFG7 – Pseudomonas putida CBB5 NdmB hexamer

Methylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N3-demethylase NdmB hexamer, 258 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
...Song HK
RgGuinier 4.3 nm
Dmax 12.2 nm

SASDFH7 – Pseudomonas putida CBB5 NdmAB complex

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 127 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
...Song HK
RgGuinier 4.2 nm
Dmax 10.9 nm

SASDFJ7 – Pseudomonas putida CBB5 mCherry-NdmA/ECFP-NdmB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 207 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 208 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
...Song HK
RgGuinier 5.6 nm
Dmax 19.1 nm

SASDJU7 – HIV-1 Primer Binding Site (PBS)-Segment RNA

Primer Binding Site-Segment experimental SAS data
DAMMIF model
Sample: Primer Binding Site-Segment monomer, 33 kDa HIV-1: pNL4-3 RNA
Buffer: 10 mM Tris, 140 mM KCl, 10 mM NaCl, 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Jul 29
The three-way junction structure of the HIV-1 PBS-segment binds host enzyme important for viral infectivity. Nucleic Acids Res (2021)
Song Z, Gremminger T, Singh G, Cheng Y, Li J, Qiu L, Ji J, Lange MJ, Zuo X, Chen SJ, Zou X, Boris-Lawrie K, Heng X
RgGuinier 3.4 nm
Dmax 12.8 nm
VolumePorod 87 nm3

SASDMU7 – Apt31 - ssDNA aptamer specific to the receptor-binding domain of SARS-CoV-2

ssDNA aptamer Apt31 specific to the receptor-binding domain of SARS-CoV-2 experimental SAS data
GROMACS model
Sample: ssDNA aptamer Apt31 specific to the receptor-binding domain of SARS-CoV-2 monomer, 10 kDa Artificially synthesized DNA
Buffer: Tris-HCl, pH: 7.4
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2020 Dec 18
Structure and Interaction Based Design of Anti‐SARS‐CoV‐2 Aptamers Chemistry – A European Journal (2022)
...Song Y, Merkuleva I, Zabluda V, Peters G, Koroleva L, Veprintsev D, Glazyrin Y, Volosnikova E, Belenkaya S, Esina T, Isaeva A, Nesmeyanova V, Shanshin D, Berlina A, Komova N, Svetlichnyi V, Silnikov V...
RgGuinier 1.9 nm
Dmax 6.5 nm
VolumePorod 12 nm3

SASDGN2 – F670E mutated dimeric bifunctional alcohol/aldehyde dehydrogenase

F670E Aldehyde-alcohol dehydrogenase experimental SAS data
SREFLEX model
Sample: F670E Aldehyde-alcohol dehydrogenase dimer, 192 kDa Escherichia coli protein
Buffer: 50 mM HEPES pH 7, 500 mM NaCl, 5% (v/v) glycerol, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Oct 4
Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity. Nat Commun 10(1):4527 (2019)
...Song JJ
RgGuinier 5.0 nm
Dmax 17.4 nm
VolumePorod 260 nm3