Browse by MODEL: Hybrid

SASDUX3 – F-actin in F-buffer at an actin concentration of 2 mg/mL

Actin, cytoplasmic 1 experimental SAS data
PYMOL model
Sample: Actin, cytoplasmic 1 18-mer, 751 kDa Gallus gallus protein
Buffer: 50 mM KCl, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2, 1 mM ATP, 0.1% 2-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Aug 31
Visualizing the nucleating and capped states of f-actin by Ca(2+)-gelsolin: Saxs data based structures of binary and ternary complexes. Int J Biol Macromol :134556 (2024)
Sagar A, Peddada N, Choudhary V, Mir Y, Garg R, Ashish
RgGuinier 13.4 nm
Dmax 48.0 nm

SASDUM5 – Mycobacterium smegmatis Inosine-5'-monophosphate dehydrogenase (IMPDH) - apo form

Inosine-5'-monophosphate dehydrogenase experimental SAS data
PYMOL model
Sample: Inosine-5'-monophosphate dehydrogenase octamer, 426 kDa Mycolicibacterium smegmatis (strain … protein
Buffer: 50 mM HEPES, 200 mM KCl, 2 mM MgCl2, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2024 Feb 21
Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase Nature Communications 15(1) (2024)
Bulvas O, Knejzlík Z, Sýs J, Filimoněnko A, Čížková M, Clarová K, Rejman D, Kouba T, Pichová I
RgGuinier 5.3 nm
Dmax 24.5 nm
VolumePorod 952 nm3

SASDUN5 – Mycobacterium smegmatis Inosine-5'-monophosphate dehydrogenase (IMPDH) - IMP-bound form

Inosine-5'-monophosphate dehydrogenase experimental SAS data
PYMOL model
Sample: Inosine-5'-monophosphate dehydrogenase tetramer, 213 kDa Mycolicibacterium smegmatis (strain … protein
Buffer: 50 mM HEPES, 200 mM KCl, 2 mM MgCl2, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2024 Mar 6
Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase Nature Communications 15(1) (2024)
Bulvas O, Knejzlík Z, Sýs J, Filimoněnko A, Čížková M, Clarová K, Rejman D, Kouba T, Pichová I
RgGuinier 5.0 nm
Dmax 21.5 nm
VolumePorod 471 nm3

SASDUP5 – Mycobacterium smegmatis Inosine-5'-monophosphate dehydrogenase (IMPDH) - ATP-bound form

Inosine-5'-monophosphate dehydrogenase experimental SAS data
PYMOL model
Sample: Inosine-5'-monophosphate dehydrogenase octamer, 426 kDa Mycolicibacterium smegmatis (strain … protein
Buffer: 50 mM HEPES, 200 mM KCl, 2 mM MgCl2, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2024 Jan 29
Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase Nature Communications 15(1) (2024)
Bulvas O, Knejzlík Z, Sýs J, Filimoněnko A, Čížková M, Clarová K, Rejman D, Kouba T, Pichová I
RgGuinier 5.0 nm
Dmax 14.8 nm
VolumePorod 821 nm3

SASDUQ5 – Mycobacterium smegmatis Inosine-5'-monophosphate dehydrogenase (IMPDH) - ATP+IMP-bound form

Inosine-5'-monophosphate dehydrogenase experimental SAS data
PYMOL model
Sample: Inosine-5'-monophosphate dehydrogenase octamer, 426 kDa Mycolicibacterium smegmatis (strain … protein
Buffer: 50 mM HEPES, 200 mM KCl, 2 mM MgCl2, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2024 Mar 6
Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase Nature Communications 15(1) (2024)
Bulvas O, Knejzlík Z, Sýs J, Filimoněnko A, Čížková M, Clarová K, Rejman D, Kouba T, Pichová I
RgGuinier 5.1 nm
Dmax 13.2 nm
VolumePorod 784 nm3

SASDUR5 – Mycobacterium smegmatis Inosine-5'-monophosphate dehydrogenase (IMPDH) - GTP-bound form

Inosine-5'-monophosphate dehydrogenase experimental SAS data
PYMOL model
Sample: Inosine-5'-monophosphate dehydrogenase octamer, 426 kDa Mycolicibacterium smegmatis (strain … protein
Buffer: 50 mM HEPES, 200 mM KCl, 2 mM MgCl2, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2024 Mar 6
Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase Nature Communications 15(1) (2024)
Bulvas O, Knejzlík Z, Sýs J, Filimoněnko A, Čížková M, Clarová K, Rejman D, Kouba T, Pichová I
RgGuinier 5.0 nm
Dmax 14.4 nm
VolumePorod 810 nm3

SASDVF2 – Staphylococcal extracellular adherence protein (Eap) in unbound form

Protein map experimental SAS data
MULTIFOXS model
Sample: Protein map monomer, 50 kDa Staphylococcus aureus (strain … protein
Buffer: 20 mM HEPES, 140 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 Jun 3
S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases. J Biol Chem 300(9):107627 (2024)
Mishra N, Gido CD, Herdendorf TJ, Hammel M, Hura GL, Fu ZQ, Geisbrecht BV
RgGuinier 4.0 nm
VolumePorod 64 nm3

SASDVG2 – Staphylococcal extracellular adherence protein (Eap) bound to human cathepsin-G

Protein mapCathepsin G experimental SAS data
MULTIFOXS model
Sample: Protein map monomer, 50 kDa Staphylococcus aureus (strain … protein
Cathepsin G tetramer, 101 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 140 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 Jun 3
S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases. J Biol Chem 300(9):107627 (2024)
Mishra N, Gido CD, Herdendorf TJ, Hammel M, Hura GL, Fu ZQ, Geisbrecht BV
RgGuinier 5.0 nm
Dmax 20.2 nm
VolumePorod 166 nm3

SASDVH2 – Staphylococcal extracellular adherence protein (Eap) bound to human neutrophil elastase

Protein mapNeutrophil elastase experimental SAS data
MULTIFOXS model
Sample: Protein map monomer, 50 kDa Staphylococcus aureus (strain … protein
Neutrophil elastase tetramer, 93 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 140 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 Dec 6
S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases. J Biol Chem 300(9):107627 (2024)
Mishra N, Gido CD, Herdendorf TJ, Hammel M, Hura GL, Fu ZQ, Geisbrecht BV
RgGuinier 4.1 nm
Dmax 10.6 nm
VolumePorod 152 nm3

SASDVK2 – Core domain of human Cathepsin-G, short truncations to both terminus (Δ22-243Δ253)

Cathepsin G experimental SAS data
PHENIX model
Sample: Cathepsin G monomer, 25 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 140 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 Jun 3
S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases. J Biol Chem 300(9):107627 (2024)
Mishra N, Gido CD, Herdendorf TJ, Hammel M, Hura GL, Fu ZQ, Geisbrecht BV
RgGuinier 1.9 nm
Dmax 6.9 nm
VolumePorod 27 nm3