Browse by MACROMOLECULE type: protein

SASDUY6 – Alarmin release inhibitor (HpARI2), full length, bound to Interleukin-33

Alarmin release inhibitor (Δ1-62)Interleukin-33 (L179V) experimental SAS data
DAMMIF model
Sample: Alarmin release inhibitor (Δ1-62) monomer, 26 kDa Heligmosomoides polygyrus protein
Interleukin-33 (L179V) monomer, 18 kDa Mus musculus protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer, 5% glycerol, pH: 7.2
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Feb 9
Structural basis for IL-33 recognition and its antagonism by the helminth effector protein HpARI2. Nat Commun 15(1):5226 (2024)
Jamwal A, Colomb F, McSorley HJ, Higgins MK
RgGuinier 2.7 nm
Dmax 9.7 nm
VolumePorod 62 nm3

SASDUZ6 – Alarmin release inhibitor (HpARI2) domains CCP2 and CCP3 bound to Interleukin-33

Interleukin-33 (L179V)Alarmin release inhibitor (Δ1-125; N175Q, N190Q) experimental SAS data
REFMAC model
Sample: Interleukin-33 (L179V) monomer, 18 kDa Mus musculus protein
Alarmin release inhibitor (Δ1-125; N175Q, N190Q) monomer, 19 kDa Heligmosomoides polygyrus protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer, 5% glycerol, pH: 7.2
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Feb 9
Structural basis for IL-33 recognition and its antagonism by the helminth effector protein HpARI2. Nat Commun 15(1):5226 (2024)
Jamwal A, Colomb F, McSorley HJ, Higgins MK
RgGuinier 2.5 nm
Dmax 8.3 nm
VolumePorod 58 nm3

SASDU47 – Non-homologous end-joining factor 1 - XLF

Non-homologous end-joining factor 1 experimental SAS data
Non-homologous end-joining factor 1 Kratky plot
Sample: Non-homologous end-joining factor 1 dimer, 67 kDa Homo sapiens protein
Buffer: 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Mar 13
Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. Nat Struct Mol Biol (2024)
Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F
RgGuinier 3.6 nm
Dmax 12.1 nm
VolumePorod 123 nm3

SASDU57 – DNA repair protein XRCC4 in complex with BRCT domains of DNA ligase 4

DNA repair protein XRCC4DNA ligase 4 experimental SAS data
DNA repair protein XRCC4 DNA ligase 4 Kratky plot
Sample: DNA repair protein XRCC4 dimer, 77 kDa Homo sapiens protein
DNA ligase 4 monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Mar 13
Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. Nat Struct Mol Biol (2024)
Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F
RgGuinier 5.8 nm
Dmax 23.0 nm
VolumePorod 248 nm3

SASDU67 – The C-terminal region of DNA repair protein XRCC4

DNA repair protein XRCC4 experimental SAS data
DNA repair protein XRCC4 Kratky plot
Sample: DNA repair protein XRCC4 monomer, 15 kDa Homo sapiens protein
Buffer: 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Oct 20
Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. Nat Struct Mol Biol (2024)
Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F
RgGuinier 3.4 nm
Dmax 11.1 nm
VolumePorod 41 nm3

SASDSE7 – Human CDAN1-interacting nuclease 1 (CDIN1): analysis of SEC peak

CDAN1-interacting nuclease 1 experimental SAS data
ALPHAFOLD model
Sample: CDAN1-interacting nuclease 1 dimer, 67 kDa Homo sapiens protein
Buffer: 20 mM Tris HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2021 Sep 2
Structural insights into inherited anemia CDA-I: disease-associated mutations disrupt Codanin1-CDIN1 complex
Tomas Brom
RgGuinier 3.0 nm
Dmax 8.2 nm
VolumePorod 84 nm3

SASDSF7 – Human Codanin1 (C-terminus): analysis of second monomeric SEC peak

Codanin-1 experimental SAS data
ALPHAFOLD model
Sample: Codanin-1 monomer, 25 kDa Homo sapiens protein
Buffer: 20 mM Tris HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Mar 5
Structural insights into inherited anemia CDA-I: disease-associated mutations disrupt Codanin1-CDIN1 complex
Tomas Brom
RgGuinier 2.7 nm
Dmax 7.5 nm
VolumePorod 54 nm3

SASDSG7 – Human Codanin1 (C-terminus): analysis of first oligomeric SEC peak

Codanin-1 experimental SAS data
ALPHAFOLD model
Sample: Codanin-1 monomer, 25 kDa Homo sapiens protein
Buffer: 20 mM Tris HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Mar 5
Structural insights into inherited anemia CDA-I: disease-associated mutations disrupt Codanin1-CDIN1 complex
Tomas Brom
RgGuinier 4.1 nm
Dmax 10.7 nm
VolumePorod 220 nm3

SASDPC4 – Complex of Rhodopseudomonas palustris pAgo with TIR-like effector protein

TIR domain-containing proteinUncharacterized protein (PIWI) experimental SAS data
ALPHAFOLD model
Sample: TIR domain-containing protein monomer, 57 kDa Rhodopseudomonas palustris (strain … protein
Uncharacterized protein (PIWI) monomer, 56 kDa Rhodopseudomonas palustris (strain … protein
Buffer: 20 mM Tris-HCl, pH8.0, 200 mM NaCl, 5 mM MgCl2, 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Sep 27
Complex of Rhodopseudomonas palustris pAgo with TIR-like effector protein
Elena Manakova
RgGuinier 3.6 nm
Dmax 12.0 nm
VolumePorod 192 nm3

SASDUG7 – Wild type Lcl C-terminal domain

HbP1 experimental SAS data
HbP1 Kratky plot
Sample: HbP1 trimer, 56 kDa Legionella pneumophila protein
Buffer: 20 mM Tris–HCl pH 8.0, 200 mM NaCl, 5 mM EDTA, pH:
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 29
The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans. Nat Commun 15(1):4912 (2024)
Rehman S, Antonovic AK, McIntire IE, Zheng H, Cleaver L, Baczynska M, Adams CO, Portlock T, Richardson K, Shaw R, Oregioni A, Mastroianni G, Whittaker SB, Kelly G, Lorenz CD, Fornili A, Cianciotto NP, Garnett JA
RgGuinier 2.8 nm
Dmax 9.7 nm
VolumePorod 105 nm3