SASDFZ3 – Escherichia coli YjhC

Escherichia coli YjhC experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Escherichia coli YjhC dimer, 86 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1 % (w/v) sodium azide, 5 % (v/v) glycerol, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 12
On the structure and function of Escherichia coli YjhC: an oxidoreductase involved in bacterial sialic acid metabolism. Proteins (2019)
Horne CR, Kind L, Davies JS, Dobson RCJ
RgGuinier 3.1 nm
Dmax 10.7 nm
VolumePorod 130 nm3

SASDGV4 – Model of the RH1-LZ1 domains of C-Jun-amino-terminal kinase-interacting protein 3 (JIP3)

C-Jun-amino-terminal kinase-interacting protein 3 experimental SAS data
OTHER model
Sample: C-Jun-amino-terminal kinase-interacting protein 3 dimer, 40 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, 0.5 mM TCEP, pH: 7.1
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Sep 22
Structural characterization of the RH1-LZI tandem of JIP3/4 highlights RH1 domains as a cytoskeletal motor-binding motif. Sci Rep 9(1):16036 (2019)
Vilela F, Velours C, Chenon M, Aumont-Nicaise M, Campanacci V, Thureau A, Pylypenko O, Andreani J, Llinas P, Ménétrey J
RgGuinier 6.3 nm
Dmax 23.1 nm
VolumePorod 140 nm3

SASDGW4 – Model of the LZ1 domain of C-Jun-amino-terminal kinase-interacting protein 3 (JIP3)

C-Jun-amino-terminal kinase-interacting protein 3 experimental SAS data
OTHER model
Sample: C-Jun-amino-terminal kinase-interacting protein 3 dimer, 40 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, 0.5 mM TCEP, pH: 7.1
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Sep 22
Structural characterization of the RH1-LZI tandem of JIP3/4 highlights RH1 domains as a cytoskeletal motor-binding motif. Sci Rep 9(1):16036 (2019)
Vilela F, Velours C, Chenon M, Aumont-Nicaise M, Campanacci V, Thureau A, Pylypenko O, Andreani J, Llinas P, Ménétrey J
RgGuinier 5.0 nm
Dmax 19.8 nm
VolumePorod 84 nm3

SASDFT4 – Conformation of the R11-15 human dystrophin fragment (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
CUSTOM IN-HOUSE model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 6.2 nm
Dmax 27.4 nm
VolumePorod 146 nm3

SASDFU4 – Conformation of R11-15 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
DAMMIF model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 6.2 nm
Dmax 28.1 nm
VolumePorod 144 nm3

SASDFV4 – Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
DAMMIF model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 8.1 nm
Dmax 29.6 nm
VolumePorod 231 nm3

SASDFW4 – Conformation of R8-15 human dystrophin fragment

Human dystrophin central domain R8-15 fragment experimental SAS data
CUSTOM IN-HOUSE model
Sample: Human dystrophin central domain R8-15 fragment monomer, 100 kDa protein
Buffer: NaP 10 mM, NaCl 500 mM, EDTA 1 mM, Glycerol 2%, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Sep 23
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 10.1 nm
Dmax 36.0 nm

SASDFX4 – Conformation of R11-19 human dystrophin fragment

Human dystrophin central domain R11-19 fragment experimental SAS data
CUSTOM IN-HOUSE model
Sample: Human dystrophin central domain R11-19 fragment monomer, 117 kDa protein
Buffer: NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycerol 2%, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 May 11
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 8.8 nm
Dmax 37.5 nm
VolumePorod 513 nm3

SASDG97 – Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN1 repeats 2-15

Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN repeats 2-15 experimental SAS data
DAMMIF model
Sample: Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN repeats 2-15 dimer, 78 kDa Trypanosoma brucei protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jan 27
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats. PLoS One 15(12):e0242677 (2020)
Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K
RgGuinier 6.5 nm
Dmax 26.0 nm
VolumePorod 187 nm3

SASDGA7 – Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN1 repeats 7-15

Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN (7-15) experimental SAS data
CUSTOM IN-HOUSE model
Sample: Trypanosoma brucei Membrane Occupation and Recognition Nexus MORN (7-15) dimer, 52 kDa Trypanosoma brucei protein
Buffer: 20 mM Tris-HCl, 200 mM NaCl, 2% (w/v) glycerol, 0.5 mM DTT, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jun 11
Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats. PLoS One 15(12):e0242677 (2020)
Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K
RgGuinier 4.1 nm
Dmax 15.5 nm
VolumePorod 56 nm3

4135 hits found.