Browse by MACROMOLECULE type: protein

SASDSS8 – Phosphorylated Calcium/calmodulin-dependent protein kinase 1 (pCaMKK1)

Calcium/calmodulin-dependent protein kinase kinase 1 (M474L) experimental SAS data
Calcium/calmodulin-dependent protein kinase kinase 1 (M474L) Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase kinase 1 (M474L) monomer, 46 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP, 3% (w/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Aug 17
14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices. Protein Sci :e4805 (2023)
Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 97 nm3

SASDST8 – Phosphorylated Calcium/calmodulin-dependent protein kinase 2 (pCaMKK2)

Calcium/calmodulin-dependent protein kinase kinase 2 experimental SAS data
Calcium/calmodulin-dependent protein kinase kinase 2 Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase kinase 2 monomer, 48 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP, 3% (w/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Aug 17
14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices. Protein Sci :e4805 (2023)
Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T
RgGuinier 3.0 nm
Dmax 12.0 nm
VolumePorod 87 nm3

SASDLC7 – Polyribonucleotide nucleotidyltransferase (PNPase): apo form

Polyribonucleotide nucleotidyltransferase experimental SAS data
DAMFILT model
Sample: Polyribonucleotide nucleotidyltransferase trimer, 246 kDa Campylobacter jejuni subsp. … protein
Buffer: 20 mM Tris-HCl, 10 mM NAH2PO4, 60 mM KCl, 1 mM MgCl2, 2 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Mar 17
Structure and function of Campylobacter jejuni polynucleotide phosphorylase (PNPase): Insights into the role of this RNase in pathogenicity. Biochimie (2023)
Bárria C, Athayde D, Hernandez G, Fonseca L, Casinhas J, Cordeiro TN, Archer M, Arraiano CM, Brito JA, Matos RG
RgGuinier 3.9 nm
Dmax 11.0 nm
VolumePorod 310 nm3

SASDLD7 – Polyribonucleotide nucleotidyltransferase (PNPase): 2-AMP complex

Polyribonucleotide nucleotidyltransferase experimental SAS data
DAMFILT model
Sample: Polyribonucleotide nucleotidyltransferase trimer, 237 kDa Campylobacter jejuni subsp. … protein
Buffer: 20 mM Tris.HCl, 10 mM NAH2PO4, 60 mM KCl, 1 mM MgCl2, 2 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Mar 17
Structure and function of Campylobacter jejuni polynucleotide phosphorylase (PNPase): Insights into the role of this RNase in pathogenicity. Biochimie (2023)
Bárria C, Athayde D, Hernandez G, Fonseca L, Casinhas J, Cordeiro TN, Archer M, Arraiano CM, Brito JA, Matos RG
RgGuinier 3.9 nm
Dmax 11.0 nm
VolumePorod 315 nm3

SASDLE7 – Polyribonucleotide nucleotidyltransferase (PNPase): 2-GMP complex

Polyribonucleotide nucleotidyltransferase experimental SAS data
DAMFILT model
Sample: Polyribonucleotide nucleotidyltransferase trimer, 237 kDa Campylobacter jejuni subsp. … protein
Buffer: 20 mM Tris.HCl, 10 mM NAH2PO4, 60 mM KCl, 1mM MgCl2, 2 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Mar 17
Structure and function of Campylobacter jejuni polynucleotide phosphorylase (PNPase): Insights into the role of this RNase in pathogenicity. Biochimie (2023)
Bárria C, Athayde D, Hernandez G, Fonseca L, Casinhas J, Cordeiro TN, Archer M, Arraiano CM, Brito JA, Matos RG
RgGuinier 3.9 nm
Dmax 11.0 nm
VolumePorod 312 nm3

SASDQY9 – Beclin-1 amino acids 1-150 with cysteine motif residues mutated to serine, along with a C-terminal tyrosine

Beclin-1 (C18S, C21S, A103V, C137S, C140S) experimental SAS data
Beclin-1 amino acids 1-150 with cysteine motif residues mutated to serine, along with a C-terminal tyrosine Rg histogram
Sample: Beclin-1 (C18S, C21S, A103V, C137S, C140S) monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM Tris, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 12
Invariant BECN1 CXXC motifs bind Zn(2+) and regulate structure and function of the BECN1 intrinsically disordered region. Autophagy :1-17 (2023)
Mukhopadhyay S, Subedi S, Hopkins JB, Ugrinov A, Chakravarthy S, Colbert CL, Sinha SC
RgGuinier 4.1 nm
Dmax 19.3 nm
VolumePorod 57 nm3

SASDQZ9 – Beclin-1 amino acids 1-150 with two cysteine motifs, along with a C-terminal tyrosine analysed using EFA in BIOXTAS RAW software, component 0

Beclin-1 experimental SAS data
Beclin-1 Kratky plot
Sample: Beclin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM Tris, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 12
Invariant BECN1 CXXC motifs bind Zn(2+) and regulate structure and function of the BECN1 intrinsically disordered region. Autophagy :1-17 (2023)
Mukhopadhyay S, Subedi S, Hopkins JB, Ugrinov A, Chakravarthy S, Colbert CL, Sinha SC
RgGuinier 4.3 nm
Dmax 20.0 nm
VolumePorod 87 nm3

SASDR22 – Beclin-1 amino acids 1-150 with two cysteine motifs, along with a C-terminal tyrosine analysed using EFA in BIOXTAS RAW software, component 1

Beclin-1 experimental SAS data
Beclin-1 amino acids 1-150 with two cysteine motifs, along with a C-terminal tyrosine analysed using EFA in BIOXTAS RAW software, component 1 Rg histogram
Sample: Beclin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM Tris, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 12
Invariant BECN1 CXXC motifs bind Zn(2+) and regulate structure and function of the BECN1 intrinsically disordered region. Autophagy :1-17 (2023)
Mukhopadhyay S, Subedi S, Hopkins JB, Ugrinov A, Chakravarthy S, Colbert CL, Sinha SC
RgGuinier 2.8 nm
Dmax 12.0 nm
VolumePorod 49 nm3

SASDJ33 – Receptor-type tyrosine-protein phosphatase epsilon bound to phospho proto-oncogene tyrosine-protein kinase (rPTPε/phospho-Src complex)

Receptor-type tyrosine-protein phosphatase epsilonProto-oncogene tyrosine-protein kinase Src, T357M mutant experimental SAS data
CORAL model
Sample: Receptor-type tyrosine-protein phosphatase epsilon monomer, 34 kDa Homo sapiens protein
Proto-oncogene tyrosine-protein kinase Src, T357M mutant monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris , 50 mM NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at 23A1, Taiwan Photon Source, NSRRC on 2017 May 26
An integrative approach unveils a distal encounter site for rPTPε and phospho-Src complex formation Structure (2023)
EswarKumar N, Yang C, Tewary S, Peng W, Chen G, Yeh Y, Yang H, Ho M
RgGuinier 2.9 nm
Dmax 10.0 nm
VolumePorod 60 nm3

SASDR96 – Human DjC20/DnaJC20/HscB iron-sulfur cluster co-chaperone protein

Iron-sulfur cluster co-chaperone protein HscB experimental SAS data
DAMMIF model
Sample: Iron-sulfur cluster co-chaperone protein HscB monomer, 25 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 50 mM NaCl, 5 mM KCl, 2 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 Aug 14
Structural characterization of the human DjC20/HscB cochaperone in solution Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics :140970 (2023)
de Souza Coto A, Pereira A, Oliveira S, de Oliveira Moritz M, da Rocha A, Dores-Silva P, da Silva N, de Araújo Nogueira A, Gava L, Seraphim T, Borges J
RgGuinier 2.5 nm
Dmax 9.0 nm
VolumePorod 40 nm3