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11 hits found for Caliandro

SASDSF2 – K48-linked diubiquitin

Polyubiquitin-C experimental SAS data
OTHER model
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
Stretching the chains: the destabilizing impact of Cu(2+) and Zn(2+) ions on K48-linked diubiquitin. Dalton Trans (2023)
...Caliandro R, Milardi D
RgGuinier 1.9 nm
Dmax 6.5 nm
VolumePorod 22 nm3

SASDSG2 – K48-linked diubiquitin in the presence of zinc ion

Polyubiquitin-C experimental SAS data
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
Stretching the chains: the destabilizing impact of Cu(2+) and Zn(2+) ions on K48-linked diubiquitin. Dalton Trans (2023)
...Caliandro R, Milardi D
RgGuinier 2.0 nm
Dmax 7.5 nm
VolumePorod 20 nm3

SASDSH2 – K48-linked diubiquitin in the presence of copper (II) ion

Polyubiquitin-C experimental SAS data
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
Stretching the chains: the destabilizing impact of Cu(2+) and Zn(2+) ions on K48-linked diubiquitin. Dalton Trans (2023)
...Caliandro R, Milardi D
RgGuinier 1.9 nm
Dmax 6.3 nm
VolumePorod 20 nm3

SASDMX3 – Anti-CD20 IgG antibody

Anti-CD20 IgG antibody (Rituximab heavy chain chimeric)Anti-CD20 IgG antibody (Rituximab light chain chimeric) experimental SAS data
Sample: Anti-CD20 IgG antibody (Rituximab heavy chain chimeric) dimer, 98 kDa Homo sapiens protein
Anti-CD20 IgG antibody (Rituximab light chain chimeric) dimer, 46 kDa Homo sapiens protein
Buffer: 100 mM HEPES, pH: 7.7
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Sep 20
Structural Characterization of the Full-Length Anti-CD20 Antibody Rituximab. Front Mol Biosci 9:823174 (2022)
...Caliandro R
RgGuinier 5.2 nm
Dmax 19.7 nm

SASDKG4 – Malus domestica double bond reductase (MdDBR) apoform

Malus domestica double bond reductase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Malus domestica double bond reductase dimer, 77 kDa Malus domestica protein
Buffer: 50 mM Tris-HCl, 100 mM NaCl., 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 2020 Oct 23
The structural and functional characterization of Malus domestica double bond reductase MdDBR provides insights towards the identification of its substrates International Journal of Biological Macromolecules 171:89-99 (2021)
Caliandro R, Polsinelli I, Demitri N, Musiani F, Martens S, Benini S
RgGuinier 3.0 nm
Dmax 9.9 nm
VolumePorod 110 nm3

SASDKH4 – Malus domestica double bond reductase in the presence of NADPH 5mM

Malus domestica double bond reductase experimental SAS data
PYMOL model
Sample: Malus domestica double bond reductase dimer, 77 kDa Malus domestica protein
Buffer: 50 mM Tris-HCl, 100 mM NaCl, 5 mM NADPH, 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 2020 Oct 23
The structural and functional characterization of Malus domestica double bond reductase MdDBR provides insights towards the identification of its substrates International Journal of Biological Macromolecules 171:89-99 (2021)
Caliandro R, Polsinelli I, Demitri N, Musiani F, Martens S, Benini S
RgGuinier 3.1 nm
Dmax 10.7 nm
VolumePorod 99 nm3

SASDR89 – Aromatic-L-amino-acid decarboxylase (AADC) - apo form

Aromatic-L-amino-acid decarboxylase (M17V) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (M17V) dimer, 108 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 28
Human aromatic amino acid decarboxylase is an asymmetric and flexible enzyme: implication in AADC deficiency Protein Science (2023)
...Caliandro R, Bertoldi M
RgGuinier 3.4 nm
Dmax 15.8 nm
VolumePorod 181 nm3

SASDR99 – Aromatic-L-amino-acid decarboxylase (AADC) - pyridoxal 5'-phosphate bound holo form

Aromatic-L-amino-acid decarboxylase (M17V) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (M17V) dimer, 108 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 28
Human aromatic amino acid decarboxylase is an asymmetric and flexible enzyme: implication in AADC deficiency Protein Science (2023)
...Caliandro R, Bertoldi M
RgGuinier 3.2 nm
Dmax 14.9 nm
VolumePorod 180 nm3

SASDRA9 – Aromatic-L-amino-acid decarboxylase (AADC) - dopa methylester DME-bound holo form

Aromatic-L-amino-acid decarboxylase (M17V) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (M17V) dimer, 108 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 28
Human aromatic amino acid decarboxylase is an asymmetric and flexible enzyme: implication in AADC deficiency Protein Science (2023)
...Caliandro R, Bertoldi M
RgGuinier 3.0 nm
Dmax 14.5 nm
VolumePorod 154 nm3

SASDNL8 – The C-terminal region of histone-lysine N-methyltransferase NSD3: PWWP2-SET construct

Histone-lysine N-methyltransferase NSD3 experimental SAS data
OTHER model
Sample: Histone-lysine N-methyltransferase NSD3 monomer, 43 kDa Homo sapiens protein
Buffer: 0.5 M NaCl, 20 mM Tris-HCl, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Nov 25
Structural insights into the C-terminus of the histone-lysine N-methyltransferase NSD3 by small-angle X-ray scattering. Front Mol Biosci 11:1191246 (2024)
...Caliandro R
RgGuinier 3.1 nm
Dmax 11.2 nm
VolumePorod 64 nm3

SASDNK8 – The C-terminal region of histone-lysine N-methyltransferase NSD3: SET-PHD4 construct

Histone-lysine N-methyltransferase NSD3 experimental SAS data
OTHER model
Sample: Histone-lysine N-methyltransferase NSD3 monomer, 40 kDa Homo sapiens protein
Buffer: 0.5 M NaCl, 20 mM Tris-HCl, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Nov 25
Structural insights into the C-terminus of the histone-lysine N-methyltransferase NSD3 by small-angle X-ray scattering. Front Mol Biosci 11:1191246 (2024)
...Caliandro R
RgGuinier 3.4 nm
Dmax 13.2 nm
VolumePorod 75 nm3