Browse by MACROMOLECULE type: protein

SASDQU9 – His-Tagged Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] in complex with His-tagged fourth BRC repeat (BRC4)

DNA repair protein RAD51 homolog 1 (F86E, A89E, His-Tagged)Breast cancer type 2 susceptibility protein experimental SAS data
His-Tagged Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] in complex with His-tagged fourth BRC repeat (BRC4) Rg histogram
Sample: DNA repair protein RAD51 homolog 1 (F86E, A89E, His-Tagged) monomer, 40 kDa Homo sapiens protein
Breast cancer type 2 susceptibility protein monomer, 6 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 200 mM Na2SO4, 5% glycerol, 0.1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Apr 7
Isolation and characterization of monomeric human RAD51: a novel tool for investigating homologous recombination in cancer Angewandte Chemie International Edition (2023)
Rinaldi F, Schipani F, Balboni B, Catalano F, Marotta R, Myers S, Previtali V, Veronesi M, Scietti L, Cecatiello V, Pasqualato S, Ortega J, Girotto S, Cavalli A
RgGuinier 3.0 nm
Dmax 16.5 nm
VolumePorod 78 nm3

SASDSN7 – Full length human mature gelsolin in closed state

Gelsolin experimental SAS data
GROMACS model
Sample: Gelsolin monomer, 85 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, 1 mM EDTA, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Feb 24
Accurate and Efficient SAXS/SANS Implementation Including Solvation Layer Effects Suitable for Molecular Simulations. J Chem Theory Comput (2023)
Ballabio F, Paissoni C, Bollati M, de Rosa M, Capelli R, Camilloni C
RgGuinier 3.2 nm
Dmax 11.1 nm
VolumePorod 128 nm3

SASDLY9 – Mouse guanylate-binding protein 7 - mGBP7

Gbp6 protein (Gbp7 - Gbp6 protein Mus musculus) experimental SAS data
GASBOR model
Sample: Gbp6 protein (Gbp7 - Gbp6 protein Mus musculus) dimer, 148 kDa Mus musculus protein
Buffer: 50 mM Tris, 5 mM MgCl, 2 mM DTT, pH: 8
Experiment: SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2019 Oct 2
Integrative modeling of guanylate binding protein dimers Protein Science (2023)
Schumann W, Loschwitz J, Reiners J, Degrandi D, Legewie L, Stühler K, Pfeffer K, Poschmann G, Smits S, Strodel B
RgGuinier 5.4 nm
Dmax 17.0 nm
VolumePorod 176 nm3

SASDJ95 – E3 ubiquitin-protein ligase BRE1 complexed with E2 ubiquitin conjugating enzyme RAD6

E3 ubiquitin-protein ligase BRE1Ubiquitin-conjugating enzyme E2 2 experimental SAS data
SREFLEX model
Sample: E3 ubiquitin-protein ligase BRE1 dimer, 50 kDa Saccharomyces cerevisiae (strain … protein
Ubiquitin-conjugating enzyme E2 2 monomer, 20 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 11
Structural basis for the role of C-terminus acidic tail of Saccharomyces cerevisiae ubiquitin-conjugating enzyme (Rad6) in E3 ligase (Bre1) mediated recognition of histones International Journal of Biological Macromolecules :127717 (2023)
Yadav P, Gupta M, Wazahat R, Islam Z, Tsutakawa S, Kamthan M, Kumar P
RgGuinier 4.1 nm
Dmax 10.4 nm
VolumePorod 105 nm3

SASDJA5 – E2 ubiquitin conjugating enzyme RAD6

Ubiquitin-conjugating enzyme E2 2 experimental SAS data
SREFLEX model
Sample: Ubiquitin-conjugating enzyme E2 2 monomer, 20 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 11
Structural basis for the role of C-terminus acidic tail of Saccharomyces cerevisiae ubiquitin-conjugating enzyme (Rad6) in E3 ligase (Bre1) mediated recognition of histones International Journal of Biological Macromolecules :127717 (2023)
Yadav P, Gupta M, Wazahat R, Islam Z, Tsutakawa S, Kamthan M, Kumar P
RgGuinier 2.3 nm
Dmax 6.6 nm
VolumePorod 31 nm3

SASDNP8 – High mannose contactin-2 immunoglobulin domains1-6, 1μM

Contactin-2 experimental SAS data
Contactin-2 Kratky plot
Sample: Contactin-2 dimer, 150 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 17
Contactin 2 homophilic adhesion structure and conformational plasticity Structure (2023)
Chataigner L, Thärichen L, Beugelink J, Granneman J, Mokiem N, Snijder J, Förster F, Janssen B
RgGuinier 5.1 nm
Dmax 20.0 nm
VolumePorod 140 nm3

SASDNQ8 – High mannose contactin 2 immunoglobulin domains1-6, 3μM

Contactin-2 experimental SAS data
Contactin-2 Kratky plot
Sample: Contactin-2 dimer, 150 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 17
Contactin 2 homophilic adhesion structure and conformational plasticity Structure (2023)
Chataigner L, Thärichen L, Beugelink J, Granneman J, Mokiem N, Snijder J, Förster F, Janssen B
RgGuinier 5.3 nm
Dmax 20.0 nm
VolumePorod 300 nm3

SASDNR8 – High mannose contactin-2 immunoglobulin domains1-6, 6μM

Contactin-2 experimental SAS data
Contactin-2 Kratky plot
Sample: Contactin-2 dimer, 150 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 17
Contactin 2 homophilic adhesion structure and conformational plasticity Structure (2023)
Chataigner L, Thärichen L, Beugelink J, Granneman J, Mokiem N, Snijder J, Förster F, Janssen B
RgGuinier 5.4 nm
Dmax 21.0 nm
VolumePorod 325 nm3

SASDNS8 – High mannose contactin-2 immunoglobulin domains1-6, 13μM

Contactin-2 experimental SAS data
Contactin-2 Kratky plot
Sample: Contactin-2 dimer, 150 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 17
Contactin 2 homophilic adhesion structure and conformational plasticity Structure (2023)
Chataigner L, Thärichen L, Beugelink J, Granneman J, Mokiem N, Snijder J, Förster F, Janssen B
RgGuinier 5.5 nm
Dmax 21.4 nm
VolumePorod 350 nm3

SASDNT8 – High mannose contactin-2 immunoglobulin domains1-6, 26μM

Contactin-2 experimental SAS data
Contactin-2 Kratky plot
Sample: Contactin-2 dimer, 150 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 17
Contactin 2 homophilic adhesion structure and conformational plasticity Structure (2023)
Chataigner L, Thärichen L, Beugelink J, Granneman J, Mokiem N, Snijder J, Förster F, Janssen B
RgGuinier 6.0 nm
Dmax 30.0 nm
VolumePorod 380 nm3