SASBDB entries for UniProt ID:

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

UniProt ID: Q13426 (1-336) DNA repair protein XRCC4

UniProt ID: P49917 (643-911) 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

UniProt ID: Q13426 (201-336) 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

SASDUG7 – Wild type Lcl C-terminal domain

UniProt ID: E7BLH6 (387-536) HbP1
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

SASDUH7 – Lcl C-terminal domain R477A mutant - trimer

UniProt ID: E7BLH6 (387-536) HbP1 (R477A)
HbP1 (R477A) experimental SAS data
HbP1 (R477A) Kratky plot
Sample: HbP1 (R477A) trimer, 55 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 2.7 nm
Dmax 9.4 nm
VolumePorod 79 nm3

SASDUJ7 – Lcl C-terminal domain R477A mutant - monomer

UniProt ID: E7BLH6 (387-536) HbP1 (R477A)
HbP1 (R477A) experimental SAS data
HbP1 (R477A) Kratky plot
Sample: HbP1 (R477A) monomer, 18 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 1.9 nm
Dmax 6.4 nm
VolumePorod 33 nm3

SASDUK7 – Lcl C-terminal domain E503A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (E503A)
HbP1 (E503A) experimental SAS data
HbP1 (E503A) Kratky plot
Sample: HbP1 (E503A) 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 9.9 nm
VolumePorod 106 nm3

SASDUL7 – Lcl C-terminal domain K504A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (K504A)
HbP1 (K504A) experimental SAS data
HbP1 (K504A) Kratky plot
Sample: HbP1 (K504A) 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 106 nm3

SASDUM7 – Lcl C-terminal domain K515A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (K515A)
HbP1 (K515A) experimental SAS data
HbP1 (K515A) Kratky plot
Sample: HbP1 (K515A) 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 9.8 nm
VolumePorod 105 nm3

SASDUN7 – Lcl C-terminal domain K520A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (K520A)
HbP1 (K520A) experimental SAS data
HbP1 (K520A) Kratky plot
Sample: HbP1 (K520A) 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 9.8 nm
VolumePorod 100 nm3

SASDUP7 – Lcl C-terminal domain D521A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (D521A)
HbP1 (D521A) experimental SAS data
HbP1 (D521A) Kratky plot
Sample: HbP1 (D521A) 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 9.8 nm
VolumePorod 108 nm3