Browse by DISSEMINATION: Published

SASDLV6 – High mannose glycan contactin 1 ectodomain, 20.5 μM

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 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 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 7.0 nm
Dmax 34.0 nm
VolumePorod 285 nm3

SASDLW6 – High mannose glycan contactin 1 ectodomain, 11.1 μM

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 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 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 6.8 nm
Dmax 27.0 nm
VolumePorod 275 nm3

SASDLX6 – High mannose glycan contactin 1 ectodomain, 5.5 μM

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 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 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 6.8 nm
Dmax 27.0 nm
VolumePorod 270 nm3

SASDLY6 – High mannose glycan contactin 1 ectodomain, 2.4 μM

Contactin-1 I433V experimental SAS data
CUSTOM IN-HOUSE model
Sample: Contactin-1 I433V dimer, 220 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 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 6.8 nm
Dmax 19.5 nm
VolumePorod 254 nm3

SASDFE6 – Sliding beta clamp

Beta sliding clamp experimental SAS data
GASBOR model
Sample: Beta sliding clamp dimer, 86 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris pH 8.0, 200 mM NaCl , 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 15
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex International Journal of Biological Macromolecules (2022)
Shukla A, Afsar M, Khanam T, Kumar N, Ali F, Kumar S, Jahan F, Ramachandran R
RgGuinier 3.7 nm
Dmax 10.3 nm
VolumePorod 186 nm3

SASDFF6 – Probable exodeoxyribonuclease III protein XthA, sliding beta clamp complex

Beta sliding clampProbable exodeoxyribonuclease III protein XthA (Exonuclease III) (EXO III) (AP endonuclease VI) experimental SAS data
DAMMIF model
Sample: Beta sliding clamp dimer, 86 kDa Mycobacterium tuberculosis protein
Probable exodeoxyribonuclease III protein XthA (Exonuclease III) (EXO III) (AP endonuclease VI) monomer, 33 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 15
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex International Journal of Biological Macromolecules (2022)
Shukla A, Afsar M, Khanam T, Kumar N, Ali F, Kumar S, Jahan F, Ramachandran R
RgGuinier 3.5 nm
Dmax 11.3 nm
VolumePorod 98 nm3

SASDFG6 – Probable exodeoxyribonuclease III protein XthA, sliding beta clamp, DNA ligase-A tricomplex

Beta sliding clampProbable exodeoxyribonuclease III protein XthADNA ligase A experimental SAS data
DAMMIF model
Sample: Beta sliding clamp dimer, 86 kDa Mycobacterium tuberculosis protein
Probable exodeoxyribonuclease III protein XthA monomer, 31 kDa Mycobacterium tuberculosis protein
DNA ligase A monomer, 76 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 17
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex International Journal of Biological Macromolecules (2022)
Shukla A, Afsar M, Khanam T, Kumar N, Ali F, Kumar S, Jahan F, Ramachandran R
RgGuinier 5.8 nm
Dmax 25.3 nm
VolumePorod 501 nm3

SASDFH6 – Probable exodeoxyribonuclease III protein XthA, sliding beta clamp, DNA ligase-A tricomplex in the presence of DNA substrate

Probable exodeoxyribonuclease III protein XthADNA ligase ABeta sliding clampDNA ligase A nicked DNA substrate experimental SAS data
DAMMIF model
Sample: Probable exodeoxyribonuclease III protein XthA monomer, 31 kDa Mycobacterium tuberculosis protein
DNA ligase A monomer, 76 kDa Mycobacterium tuberculosis protein
Beta sliding clamp dimer, 86 kDa Mycobacterium tuberculosis protein
DNA ligase A nicked DNA substrate dimer, 16 kDa DNA
Buffer: 50 mM Tris pH 8.0, 200 mM NaCl , 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 17
Regulation of futile ligation during early steps of BER in M. tuberculosis is carried out by a β-clamp-XthA-LigA tri-component complex International Journal of Biological Macromolecules (2022)
Shukla A, Afsar M, Khanam T, Kumar N, Ali F, Kumar S, Jahan F, Ramachandran R
RgGuinier 5.8 nm
Dmax 19.1 nm
VolumePorod 496 nm3

SASDPF3 – Receptor-type tyrosine-protein phosphatase kappa extracellular domains (PTPRK-ECDs)

Receptor-type tyrosine-protein phosphatase kappa experimental SAS data
DAMMIN model
Sample: Receptor-type tyrosine-protein phosphatase kappa monomer, 82 kDa Homo sapiens protein
Buffer: 50 mM MES, 250 mM NaCl, 3% v/v glycerol,, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Dec 13
Determinants of receptor tyrosine phosphatase homophilic adhesion: structural comparison of PTPRK and PTPRM extracellular domains Journal of Biological Chemistry :102750 (2022)
Hay I, Shamin M, Caroe E, Mohammed A, Svergun D, Jeffries C, Graham S, Sharpe H, Deane J
RgGuinier 7.0 nm
Dmax 26.0 nm
VolumePorod 252 nm3

SASDPG3 – Receptor-type tyrosine-protein phosphatase mu extracellular domains (PTPRM-ECDs)

Receptor-type tyrosine-protein phosphatase mu experimental SAS data
DAMMIN model
Sample: Receptor-type tyrosine-protein phosphatase mu monomer, 82 kDa Homo sapiens protein
Buffer: 50 mM MES, 250 mM NaCl, 3% v/v glycerol,, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Dec 13
Determinants of receptor tyrosine phosphatase homophilic adhesion: structural comparison of PTPRK and PTPRM extracellular domains Journal of Biological Chemistry :102750 (2022)
Hay I, Shamin M, Caroe E, Mohammed A, Svergun D, Jeffries C, Graham S, Sharpe H, Deane J
RgGuinier 7.2 nm
Dmax 26.0 nm
VolumePorod 255 nm3