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SASDMK4 – Fe3O4 nanoparticles (radius 5.6 nm )

Fe3O4 nanoparticles; radius 5.6 nm (AFM based) experimental SAS data
Fe3O4 nanoparticles; radius 5.6 nm (AFM based) Kratky plot
Sample: Fe3O4 nanoparticles; radius 5.6 nm (AFM based) monomer, 1 kDa
Buffer: water, HCLO4, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Sep 5
Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites. Biopolymers 111(2):e23342 (2020)
Majorošová J, Schroer MA, Tomašovičová N, Batková M, Hu PS, Kubovčíková M, Svergun DI, Kopčanský P
RgGuinier 11.0 nm
Dmax 20.0 nm

SASDML4 – LAF + MNP (r = 5.6 nm) nanocomposite

lysozyme amyloid fibrilFe3O4 nanoparticles; radius 5.6 nm (AFM based) experimental SAS data
DAMMIF model
Sample: Lysozyme amyloid fibril, 1 kDa Gallus gallus protein
Fe3O4 nanoparticles; radius 5.6 nm (AFM based) monomer, 1 kDa
Buffer: 0.2 M glycine-HCl, 80 mM NaCl, pH: 2.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Sep 8
Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites. Biopolymers 111(2):e23342 (2020)
Majorošová J, Schroer MA, Tomašovičová N, Batková M, Hu PS, Kubovčíková M, Svergun DI, Kopčanský P
RgGuinier 29.4 nm
Dmax 80.0 nm

SASDF85 – Pseudomonas aeruginosa antitoxin HigA: apo PaHigA

Uncharacterized protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Uncharacterized protein dimer, 22 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Tris, 300 mM NaCl, 5% (v/v) glycerol, and 1 mM PMSF, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Dec 21
Structural Insights Into the Transcriptional Regulation of HigBA Toxin–Antitoxin System by Antitoxin HigA in Pseudomonas aeruginosa Frontiers in Microbiology 10 (2020)
Liu Y, Gao Z, Liu G, Geng Z, Dong Y, Zhang H
RgGuinier 2.0 nm
Dmax 6.6 nm
VolumePorod 23 nm3

SASDF95 – Pseudomonas aeruginosa antitoxin HigA bound to duplex DNA: PaHigA-DNA complex

Uncharacterized proteinDNA Duplex experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Uncharacterized protein dimer, 22 kDa Pseudomonas aeruginosa protein
DNA Duplex dimer, 20 kDa DNA
Buffer: 20 mM Tris, 300 mM NaCl, 5% (v/v) glycerol, and 1 mM PMSF, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Sep 19
Structural Insights Into the Transcriptional Regulation of HigBA Toxin–Antitoxin System by Antitoxin HigA in Pseudomonas aeruginosa Frontiers in Microbiology 10 (2020)
Liu Y, Gao Z, Liu G, Geng Z, Dong Y, Zhang H
RgGuinier 2.9 nm
Dmax 9.8 nm
VolumePorod 81 nm3

SASDHW3 – Binary-patterned 4-helix bundle de novo protein WA20

De novo protein WA20 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: De novo protein 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-6A, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2016 Feb 26
Hyperstable De Novo Protein with a Dimeric Bisecting Topology. ACS Synth Biol (2020)
Kimura N, Mochizuki K, Umezawa K, Hecht MH, Arai R
RgGuinier 2.7 nm
Dmax 10.0 nm

SASDHX3 – Hyperstable de novo protein Super WA20 (SUWA)

Hyperstable de novo protein Super WA20 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Hyperstable de novo protein Super 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-6A, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2016 Feb 26
Hyperstable De Novo Protein with a Dimeric Bisecting Topology. ACS Synth Biol (2020)
Kimura N, Mochizuki K, Umezawa K, Hecht MH, Arai R
RgGuinier 2.7 nm
Dmax 10.0 nm

SASDGS5 – MvaT (low salt data set)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 50 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.6 nm
Dmax 14.7 nm
VolumePorod 47 nm3

SASDGT5 – MvaT (high salt data set)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 300 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.8 nm
Dmax 15.8 nm
VolumePorod 50 nm3

SASDG95 – Phosphorylated resistance to inhibitors of cholinesterase 8 homolog A (Ric-8A, 1-491) and G protein complex

Resistance to inhibitors of cholinesterase 8 homolog AGuanine nucleotide-binding protein G(i) subunit alpha-1 experimental SAS data
DAMMIF model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Rattus norvegicus protein
Guanine nucleotide-binding protein G(i) subunit alpha-1 monomer, 38 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jul 30
Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1 Nature Communications 11(1) (2020)
McClelland L, Zhang K, Mou T, Johnston J, Yates-Hansen C, Li S, Thomas C, Doukov T, Triest S, Wohlkonig A, Tall G, Steyaert J, Chiu W, Sprang S
RgGuinier 3.5 nm
Dmax 11.5 nm
VolumePorod 120 nm3

SASDHP7 – Haloalkane dehalogenase variant DhaA115 - monomeric fraction

Haloalkane dehalogenase variant DhaA115 -monomeric fraction experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Haloalkane dehalogenase variant DhaA115 -monomeric fraction monomer, 34 kDa Rhodococcus rhodochrous protein
Buffer: 50 mM potassium phosphate buffer (41 mM K₂HPO₄, 9mM KH₂PO₄), pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2019 Aug 22
Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst Chemical Science 11(41):11162-11178 (2020)
Markova K, Chmelova K, Marques S, Carpentier P, Bednar D, Damborsky J, Marek M
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 41 nm3