Browse by ORGANISM: other species

SASDBF7 – Dps2, DNA binding protein under starvation conditions (SEC-SAXS)

N-terminal truncated DNA protection during starvation protein 2 experimental SAS data
EOM/RANCH model
Sample: N-terminal truncated DNA protection during starvation protein 2 dodecamer, 279 kDa Deinococcus radiodurans R1 protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV
RgGuinier 4.2 nm
Dmax 12.7 nm
VolumePorod 445 nm3

SASDBG7 – Dps1, DNA binding protein under starvation conditions (SEC-SAXS)

DNA protection during starvation protein 1 experimental SAS data
GASBOR model
Sample: DNA protection during starvation protein 1 dodecamer, 276 kDa Deinococcus radiodurans R1 protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV
RgGuinier 4.2 nm
Dmax 12.8 nm
VolumePorod 437 nm3

SASDBH7 – Dps1 truncated, DNA binding protein under starvation conditions (SEC-SAXS)

N-terminal truncated DNA protection during starvation protein 1 experimental SAS data
GASBOR model
Sample: N-terminal truncated DNA protection during starvation protein 1 dodecamer, 216 kDa Deinococcus radiodurans R1 protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV
RgGuinier 3.9 nm
Dmax 10.0 nm
VolumePorod 291 nm3

SASDDH7 – Citrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA in the presence of citrate

citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA experimental SAS data
GROMACS model
Sample: Citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA dimer, 77 kDa protein
Buffer: 10 mM glycine buffer, 10 mM NaCl, 1 mM sodium citrate, pH: 10
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 6
A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase. Sci Rep 7:42592 (2017)
Kaschner M, Schillinger O, Fettweiss T, Nutschel C, Krause F, Fulton A, Strodel B, Stadler A, Jaeger KE, Krauss U
RgGuinier 3.3 nm
Dmax 11.7 nm

SASDDJ7 – Citrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA

citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA experimental SAS data
DAMMIF model
Sample: Citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA dimer, 77 kDa protein
Buffer: 10 mM glycine buffer, 10 mM NaCl, pH: 10
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 6
A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase. Sci Rep 7:42592 (2017)
Kaschner M, Schillinger O, Fettweiss T, Nutschel C, Krause F, Fulton A, Strodel B, Stadler A, Jaeger KE, Krauss U
RgGuinier 3.3 nm
Dmax 11.8 nm

SASDAY8 – Human alphacoronavirus non-structural protein Nsp10 in the presence of Zn

HCoV-229E Non-structural protein 10 experimental SAS data
CORAL model
Sample: HCoV-229E Non-structural protein 10 monomer, 15 kDa Human coronavirus 229E protein
Buffer: 25 mM HEPES 280 mM NaCl 2 mM DTT 500 µM ZnCl2, pH: 7.6
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 25
Human alphacoronavirus non-structural protein Nsp10
Sven Falke, Al Kikhney
RgGuinier 1.7 nm
Dmax 5.8 nm

SASDA39 – HCoV-229E Nsp10 in the absence of Zn

HCoV-229E Non-structural protein 10 experimental SAS data
CORAL model
Sample: HCoV-229E Non-structural protein 10 monomer, 15 kDa Human coronavirus 229E protein
Buffer: 25 mM HEPES 400 mM NaCl 1 mM EDTA 5% glycerol 40 mM NaH2PO4, pH: 7.9
Experiment: SAXS data collected at EMBL P12, PETRA III on 2011 Sep 8
Human alphacoronavirus non-structural protein Nsp10
Sven Falke, Al Kikhney
RgGuinier 1.9 nm
Dmax 6.9 nm

SASDB65 – Tyrosine-protein phosphatase (YopH)/putative yopH targeting protein (SycH) heterotrimeric complex

SycH putative yopH targeting proteinTyrosine-protein phosphatase YopH experimental SAS data
CRYSOL model
Sample: SycH putative yopH targeting protein dimer, 32 kDa Yersinia pseudotuberculosis protein
Tyrosine-protein phosphatase YopH monomer, 14 kDa Yersinia pseudotuberculosis protein
Buffer: 50 mM HEPES 2mM TCEP, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Aug 1
Global Disordering in Stereo-Specific Protein Association Biophysical Journal 112(3):33a (2017)
Gupta A, Reinartz I, Spilotros A, Jonna V, Hofer A, Svergun D, Schug A, Wolf-Watz M
RgGuinier 3.0 nm
Dmax 12.5 nm
VolumePorod 89 nm3

SASDBP4 – Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD

Iron-regulated outer membrane lipoprotein FrpD experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Buffer: 10 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Oct 19
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis. Sci Rep 7:40408 (2017)
Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L
RgGuinier 2.2 nm
Dmax 6.5 nm
VolumePorod 41 nm3

SASDBQ4 – Neisseria meningitidis iron-regulated FrpD-FrpC lipoprotein/protein complex

Iron-regulated outer membrane lipoprotein FrpDIron-regulated protein FrpC experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Iron-regulated protein FrpC monomer, 46 kDa Neisseria meningitidis protein
Buffer: 50 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Oct 19
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis. Sci Rep 7:40408 (2017)
Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L
RgGuinier 3.7 nm
Dmax 13.5 nm
VolumePorod 123 nm3