Browse by ORGANISM: other species

SASDP49 – BTB domain of CG6765 protein at 1.5 mg/ml

Uncharacterized protein, isoform A experimental SAS data
ALPHAFOLD model
Sample: Uncharacterized protein, isoform A hexamer, 92 kDa Drosophila melanogaster protein
Buffer: 20 mM Tris, pH 7.4, 200 mM NaCl, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Jul 20
The Arthropoda-specific Tramtrack group BTB protein domains use previously unknown interface to form hexamers. Elife 13 (2024)
Bonchuk AN, Balagurov KI, Baradaran R, Boyko KM, Sluchanko NN, Khrustaleva AM, Burtseva AD, Arkova OV, Khalisova KK, Popov VO, Naschberger A, Georgiev PG
RgGuinier 3.7 nm
Dmax 12.7 nm
VolumePorod 166 nm3

SASDP59 – BTB domain of longitudinals lacking (LOLA) protein

Longitudinals lacking protein, isoform G experimental SAS data
ALPHAFOLD model
Sample: Longitudinals lacking protein, isoform G hexamer, 92 kDa Drosophila melanogaster protein
Buffer: 20 mM Tris, pH 7.4, 200 mM NaCl, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Jul 20
The Arthropoda-specific Tramtrack group BTB protein domains use previously unknown interface to form hexamers. Elife 13 (2024)
Bonchuk AN, Balagurov KI, Baradaran R, Boyko KM, Sluchanko NN, Khrustaleva AM, Burtseva AD, Arkova OV, Khalisova KK, Popov VO, Naschberger A, Georgiev PG
RgGuinier 4.1 nm
Dmax 14.5 nm
VolumePorod 189 nm3

SASDSN8 – Pro-Nivolumab, Lu02

Pro-Nivolumab, Lu02 experimental SAS data
AMBER model
Sample: Pro-Nivolumab, Lu02 monomer, 54 kDa protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at TPS13A, NSRRC on 2022 Sep 8
Integrating molecular dynamics simulation with small- and wide-angle X-ray scattering to unravel the flexibility, antigen-blocking, and protease-restoring functions in a hindrance-based pro-antibody. Protein Sci 33(9):e5124 (2024)
Liao JM, Hong ST, Wang YT, Cheng YA, Ho KW, Toh SI, Shih O, Jeng US, Lyu PC, Hu IC, Huang MY, Chang CY, Cheng TL
RgGuinier 3.0 nm
Dmax 11.5 nm
VolumePorod 69 nm3

SASDTX8 – Streptococcus pyogenes glycine cleavage system H-like protein

Glycine cleavage system H-like protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Glycine cleavage system H-like protein monomer, 13 kDa Streptococcus pyogenes serotype … protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT, 5% (v/v) glycerol, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jul 20
Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains Journal of Biological Chemistry :107770 (2024)
Ariza A, Liu Q, Cowieson N, Ahel I, Filippov D, Rack J
RgGuinier 1.5 nm
Dmax 5.0 nm
VolumePorod 22 nm3

SASDTY8 – Streptococcus pyogenes Protein-ADP-ribose hydrolase

Protein-ADP-ribose hydrolase (D13G, Y23S, T61A, I114S, R177H, I246T) experimental SAS data
ALPHAFOLD model
Sample: Protein-ADP-ribose hydrolase (D13G, Y23S, T61A, I114S, R177H, I246T) monomer, 30 kDa Streptococcus pyogenes serotype … protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT, 5% (v/v) glycerol, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jul 20
Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains Journal of Biological Chemistry :107770 (2024)
Ariza A, Liu Q, Cowieson N, Ahel I, Filippov D, Rack J
RgGuinier 2.1 nm
Dmax 7.3 nm
VolumePorod 34 nm3

SASDTZ8 – Streptococcus pyogenes Protein-ADP-ribose hydrolase: glycine cleavage system H-like protein complex

Glycine cleavage system H-like proteinProtein-ADP-ribose hydrolase (D13G, Y23S, T61A, I114S, R177H, I246T) experimental SAS data
ALPHAFOLD model
Sample: Glycine cleavage system H-like protein monomer, 13 kDa Streptococcus pyogenes serotype … protein
Protein-ADP-ribose hydrolase (D13G, Y23S, T61A, I114S, R177H, I246T) monomer, 30 kDa Streptococcus pyogenes serotype … protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT, 5% (v/v) glycerol, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jul 20
Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains Journal of Biological Chemistry :107770 (2024)
Ariza A, Liu Q, Cowieson N, Ahel I, Filippov D, Rack J
RgGuinier 2.4 nm
Dmax 8.4 nm
VolumePorod 53 nm3

SASDTL2 – V3 variant of the low complexity domain of hnRNPA1 (Heterogeneous nuclear ribonucleoprotein A1)

V3 variant of the low complexity domain of hnRNPA1 experimental SAS data
V3 variant of the low complexity domain of hnRNPA1 Kratky plot
Sample: V3 variant of the low complexity domain of hnRNPA1 monomer, 13 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Nov 19
Design of intrinsically disordered protein variants with diverse structural properties Science Advances 10(35) (2024)
Pesce F, Bremer A, Tesei G, Hopkins J, Grace C, Mittag T, Lindorff-Larsen K
RgGuinier 2.3 nm
Dmax 9.3 nm
VolumePorod 18 nm3

SASDTM2 – V4 variant of the low complexity domain of hnRNPA1 (Heterogeneous nuclear ribonucleoprotein A1)

V4 variant of the low complexity domain of hnRNPA1 experimental SAS data
V4 variant of the low complexity domain of hnRNPA1 Kratky plot
Sample: V4 variant of the low complexity domain of hnRNPA1 monomer, 13 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Nov 19
Design of intrinsically disordered protein variants with diverse structural properties Science Advances 10(35) (2024)
Pesce F, Bremer A, Tesei G, Hopkins J, Grace C, Mittag T, Lindorff-Larsen K
RgGuinier 2.4 nm
Dmax 9.9 nm
VolumePorod 19 nm3

SASDTN2 – V5 variant of the low complexity domain of hnRNPA1 (Heterogeneous nuclear ribonucleoprotein A1)

V5 variant of the low complexity domain of hnRNPA1 experimental SAS data
V5 variant of the low complexity domain of hnRNPA1 Kratky plot
Sample: V5 variant of the low complexity domain of hnRNPA1 monomer, 13 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Nov 19
Design of intrinsically disordered protein variants with diverse structural properties Science Advances 10(35) (2024)
Pesce F, Bremer A, Tesei G, Hopkins J, Grace C, Mittag T, Lindorff-Larsen K
RgGuinier 2.5 nm
Dmax 9.5 nm
VolumePorod 19 nm3

SASDTQ5 – SemDΔAPH (apo form)

Uncharacterized protein experimental SAS data
CORAL model
Sample: Uncharacterized protein monomer, 35 kDa Chlamydia pneumoniae protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, 3 %Glycerol, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Dec 14
The Chlamydia pneumoniae effector SemD exploits its host’s endocytic machinery by structural and functional mimicry Nature Communications 15(1) (2024)
Kocher F, Applegate V, Reiners J, Port A, Spona D, Hänsch S, Mirzaiebadizi A, Ahmadian M, Smits S, Hegemann J, Mölleken K
RgGuinier 2.8 nm
Dmax 10.5 nm
VolumePorod 67 nm3