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8 hits found for Bumba

SASDJS3 – Adenylate cyclase toxin CyaA RTX block II-V

Bifunctional hemolysin/adenylate cyclase experimental SAS data
DAMMIF model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 57 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins. J Mol Biol (2020)
...Bumba L
RgGuinier 4.0 nm
Dmax 13.3 nm
VolumePorod 94 nm3

SASDJT3 – Adenylate cyclase toxin CyaA RTX block III-V

Bifunctional hemolysin/adenylate cyclase experimental SAS data
DAMMIF model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 45 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins. J Mol Biol (2020)
...Bumba L
RgGuinier 3.4 nm
Dmax 12.1 nm
VolumePorod 85 nm3

SASDJU3 – Adenylate cyclase toxin CyaA RTX block IV-V

Bifunctional hemolysin/adenylate cyclase experimental SAS data
DAMMIF model
Sample: Bifunctional hemolysin/adenylate cyclase monomer, 32 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins. J Mol Biol (2020)
...Bumba L
RgGuinier 2.7 nm
Dmax 8.6 nm
VolumePorod 45 nm3

SASDB74 – CyaA Block I-V

Adenylate cyclase toxin Block I-V experimental SAS data
DAMMIF model
Sample: Adenylate cyclase toxin Block I-V monomer, 70 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl 150 mM NaCl 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Mol Cell 62(1):47-62 (2016)
Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P
RgGuinier 5.6 nm
Dmax 17.2 nm
VolumePorod 275 nm3

SASDB84 – CyaA Block V

Adenylate cyclase toxin Block V experimental SAS data
DAMMIF model
Sample: Adenylate cyclase toxin Block V monomer, 16 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl 150 mM NaCl 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Mol Cell 62(1):47-62 (2016)
Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P
RgGuinier 1.8 nm
Dmax 5.9 nm
VolumePorod 24 nm3

SASDBP4 – Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD

Iron-regulated outer membrane lipoprotein FrpD experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Buffer: 10 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III on 2011 Oct 19
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis. Sci Rep 7:40408 (2017)
...Bumba L
RgGuinier 2.2 nm
Dmax 6.5 nm
VolumePorod 41 nm3

SASDBQ4 – Neisseria meningitidis iron-regulated FrpD-FrpC lipoprotein/protein complex

Iron-regulated outer membrane lipoprotein FrpDIron-regulated protein FrpC experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Iron-regulated protein FrpC monomer, 46 kDa Neisseria meningitidis protein
Buffer: 50 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III on 2011 Oct 19
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis. Sci Rep 7:40408 (2017)
...Bumba L
RgGuinier 3.7 nm
Dmax 13.5 nm
VolumePorod 123 nm3

SASDAG7 – CD44 HABD scFv MEM-85 complex

Hyaluronate binding domain of CD44 antigenSingle-chain Variable Fragment of Antibody MEM-85 experimental SAS data
DAMMIN model
Sample: Hyaluronate binding domain of CD44 antigen monomer, 18 kDa Homo sapiens protein
Single-chain Variable Fragment of Antibody MEM-85 monomer, 29 kDa Mus musculus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Molecular mechanism for the action of the anti-CD44 monoclonal antibody MEM-85. J Struct Biol 191(2):214-23 (2015)
...Bumba L, Svergun DI, Tošner Z, Veverka V, Řezáčová P
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 57 nm3