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20 hits found for Lorenz

SASDTC5 – Full-length E3 ubiquitin-protein ligase HACE1

E3 ubiquitin-protein ligase HACE1 experimental SAS data
GASBOR model
Sample: E3 ubiquitin-protein ligase HACE1 dimer, 205 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 50 mM NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 21
Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1 Nature Structural & Molecular Biology (2024)
...Lorenz S
RgGuinier 5.2 nm
Dmax 16.4 nm
VolumePorod 379 nm3

SASDTD5 – N-terminally truncated E3 ubiquitin-protein ligase HACE1

E3 ubiquitin-protein ligase HACE1 experimental SAS data
MULTIFOXS model
Sample: E3 ubiquitin-protein ligase HACE1 monomer, 100 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 50 mM NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 21
Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1 Nature Structural & Molecular Biology (2024)
...Lorenz S
RgGuinier 4.6 nm
Dmax 17.8 nm
VolumePorod 219 nm3

SASDDD6 – Human Guanylate-binding protein (hGBP1)

Guanylate-binding protein 1 experimental SAS data
DAMMIF model
Sample: Guanylate-binding protein 1 monomer, 68 kDa Homo sapiens protein
Buffer: 50 mM TRIS, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2018 Apr 30
Integrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase. Elife 12 (2023)
...Lorenz C, Valeri A, Folz J, Hanke CA, Ince S, Vöpel T, Farago B, Gohlke H, Klare JP, Stadler AM, Seidel CAM, Herrmann C
RgGuinier 3.9 nm
Dmax 14.4 nm
VolumePorod 105 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)
...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

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)
...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

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)
...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

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)
...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

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)
...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

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)
...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

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)
...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

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)
...Lorenz CD, Fornili A, Cianciotto NP, Garnett JA
RgGuinier 2.8 nm
Dmax 9.8 nm
VolumePorod 108 nm3

SASDUQ7 – Lcl C-terminal domain K526A mutant

HbP1 (K526A) experimental SAS data
HbP1 (K526A) Kratky plot
Sample: HbP1 (K526A) 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)
...Lorenz CD, Fornili A, Cianciotto NP, Garnett JA
RgGuinier 2.8 nm
Dmax 9.5 nm
VolumePorod 104 nm3

SASDEE8 – Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), monomer from SEC-SAXS

farnesylated human Guanylate-binding protein 1 experimental SAS data
Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), monomer from SEC-SAXS Rg histogram
Sample: farnesylated human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 102 nm3

SASDEF8 – Human Guanylate Binding Protein 1 (hGBP1), monomer from SEC-SAXS

human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 (hGBP1), monomer from SEC-SAXS Rg histogram
Sample: human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.9 nm
Dmax 13.4 nm
VolumePorod 106 nm3

SASDEG8 – Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), dimer from SEC-SAXS

human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), dimer from SEC-SAXS Rg histogram
Sample: human Guanylate-binding protein 1 dimer, 138 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 5.5 nm
Dmax 22.0 nm
VolumePorod 270 nm3

SASDEH8 – Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), monomer from SEC-SAXS

human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), monomer from SEC-SAXS Rg histogram
Sample: human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 4.5 nm
Dmax 20.5 nm
VolumePorod 120 nm3

SASDEJ8 – Human Guanylate Binding Protein 1 (hGBP1), dimer from SEC-SAXS

human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 (hGBP1), dimer from SEC-SAXS Rg histogram
Sample: human Guanylate-binding protein 1 dimer, 138 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 4.8 nm
Dmax 15.6 nm
VolumePorod 211 nm3

SASDEK8 – Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), batch mode

farnesylated human Guanylate-binding protein 1 experimental SAS data
PYMOL model
Sample: farnesylated human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2016 May 8
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.8 nm
Dmax 14.3 nm
VolumePorod 102 nm3

SASDEL8 – Human Guanylate Binding Protein 1 (hGBP1), batch mode

human Guanylate-binding protein 1 experimental SAS data
PYMOL model
Sample: human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2016 May 8
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 5.1 nm
Dmax 27.4 nm
VolumePorod 162 nm3

SASDEM8 – Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), batch mode

human Guanylate-binding protein 1 experimental SAS data
PYMOL model
Sample: human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2016 May 8
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 5.5 nm
Dmax 27.0 nm
VolumePorod 186 nm3