Browse by MACROMOLECULE type: protein

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

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)
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

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

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

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

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

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

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

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)
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 9.5 nm
VolumePorod 104 nm3

SASDSM9 – Hen egg white lysozyme in 1 mol% ethylammonium nitrate

Lysozyme C experimental SAS data
Lysozyme C Kratky plot
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 1 mol% ethylammonium nitrate, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Nov 27
Scattering approaches to unravel protein solution behaviors in ionic liquids and deep eutectic solvents: From basic principles to recent developments Advances in Colloid and Interface Science :103242 (2024)
Han Q, Veríssimo N, Bryant S, Martin A, Huang Y, Pereira J, Santos-Ebinuma V, Zhai J, Bryant G, Drummond C, Greaves T
RgGuinier 1.6 nm
Dmax 6.2 nm
VolumePorod 20 nm3