Browse by MACROMOLECULE type: protein

SASDHG4 – NopAA, a type three effector from Sinorhizobium fredii USDA257 whith xyloglucanase activity

Type III effector NopAA experimental SAS data
ALLOSMOD model
Sample: Type III effector NopAA monomer, 31 kDa Sinorhizobium fredii USDA257 protein
Buffer: PBS, 150 mM NaCl, 10% glycerol, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 17
Structural and enzymatic characterisation of the Type III effector NopAA (=GunA) from Sinorhizobium fredii USDA257 reveals a Xyloglucan hydrolase activity. Sci Rep 10(1):9932 (2020)
Dorival J, Philys S, Giuntini E, Brailly R, de Ruyck J, Czjzek M, Biondi E, Bompard C
RgGuinier 2.4 nm
Dmax 9.9 nm
VolumePorod 38 nm3

SASDH65 – Poly(rC)-binding protein 2 (PCBP2)

Poly(rC)-binding protein 2 experimental SAS data
Poly(rC)-binding protein 2 Kratky plot
Sample: Poly(rC)-binding protein 2 monomer, 40 kDa Homo sapiens protein
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Jul 16
Structure of the PCBP2/stem-loop IV complex underlying translation initiation mediated by the poliovirus type I IRES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 3.3 nm
Dmax 13.2 nm
VolumePorod 76 nm3

SASDH95 – Truncated Poly(rC)-binding protein 2 (PCBP2-ΔKH3)

Truncated poly(rC)-binding protein 2 (ΔKH3) experimental SAS data
Truncated poly(rC)-binding protein 2 (ΔKH3) Kratky plot
Sample: Truncated poly(rC)-binding protein 2 (ΔKH3) monomer, 28 kDa Homo sapiens protein
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Jan 1
Structure of the PCBP2/stem-loop IV complex underlying translation initiation mediated by the poliovirus type I IRES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 2.6 nm
Dmax 9.2 nm
VolumePorod 66 nm3

SASDHW2 – The Legionella pneumophila type II secretion system substrate NttE

Uncharacterized protein experimental SAS data
GASBOR model
Sample: Uncharacterized protein dimer, 66 kDa Legionella pneumophila protein
Buffer: 20 mM Tris, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Sep 18
Structure, Dynamics and Cellular Insight Into Novel Substrates of the Legionella pneumophila Type II Secretion System Frontiers in Molecular Biosciences 7 (2020)
Portlock T, Tyson J, Dantu S, Rehman S, White R, McIntire I, Sewell L, Richardson K, Shaw R, Pandini A, Cianciotto N, Garnett J
RgGuinier 2.9 nm
Dmax 9.4 nm
VolumePorod 114 nm3

SASDFN6 – DNA-binding protein HU-alpha

DNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: DNA-binding protein HU-alpha octamer, 77 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 3.2 nm
Dmax 10.7 nm

SASDFQ6 – DNA-binding protein HU-alpha, E34K

DNA-binding protein HU-alpha, E34K experimental SAS data
CHIMERA model
Sample: DNA-binding protein HU-alpha, E34K dimer, 19 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 2.2 nm
Dmax 6.7 nm
VolumePorod 36 nm3

SASDFW7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆328-352 (MCoA∆328-352)

Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) experimental SAS data
DAMFILT model
Sample: Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) monomer, 53 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 13
The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis ACS Catalysis (2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
RgGuinier 2.3 nm
Dmax 6.9 nm
VolumePorod 77 nm3

SASDFX7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆337-346 (MCoA∆337-346)

Aquifex aeolicus McoA metaloxidase ∆337-346 experimental SAS data
DAMMIF model
Sample: Aquifex aeolicus McoA metaloxidase ∆337-346 monomer, 54 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Dec 4
The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis ACS Catalysis (2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
RgGuinier 2.3 nm
Dmax 7.0 nm
VolumePorod 78 nm3

SASDFY7 – Aquifex aeolicus McoA metaloxidase

Aquifex aeolicus McoA metaloxidase experimental SAS data
DAMFILT model
Sample: Aquifex aeolicus McoA metaloxidase monomer, 55 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Apr 15
The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis ACS Catalysis (2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
RgGuinier 2.3 nm
Dmax 7.5 nm
VolumePorod 79 nm3

SASDH92 – Plasmodium falciparum lipocalin (PF3D7_0925900): Dimer-tetramer equilibrium through a concentration series (combined batch and SEC-SAXS measurements)

Plasmodium falciparum Lipocalin experimental SAS data
SASREF MX model
Sample: Plasmodium falciparum Lipocalin tetramer, 89 kDa Plasmodium falciparum protein
Buffer: 20 mM Tris pH7.5, 150 mM NaCl, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Apr 8
Structure-Based Identification and Functional Characterization of a Lipocalin in the Malaria Parasite Plasmodium falciparum Cell Reports 31(12):107817 (2020)
Burda P, Crosskey T, Lauk K, Zurborg A, Söhnchen C, Liffner B, Wilcke L, Pietsch E, Strauss J, Jeffries C, Svergun D, Wilson D, Wilmanns M, Gilberger T
RgGuinier 3.2 nm
Dmax 10.3 nm
VolumePorod 126 nm3