SASBDB entries for UniProt ID:

SASDFC8 – Delta subunit of RNA polymerase, RNAP (B. subtilis): Lysine to glutamate mutant, 800mM NaCl

UniProt ID: P12464 (1-173) DNA-directed RNA polymerase subunit delta - mutant
DNA-directed RNA polymerase subunit delta - mutant experimental SAS data
DNA-directed RNA polymerase subunit delta - mutant Kratky plot
Sample: DNA-directed RNA polymerase subunit delta - mutant monomer, 20 kDa Bacillus subtilis protein
Buffer: 20 mM Phosphate buffer, 800 mM NaCl, 0.05% NaN3, pH: 6.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 3
Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. J Am Chem Soc (2019)
Kuban V, Srb P, Stegnerova H, Padrta P, Zachrdla M, Jasenakova Z, Šanderová H, Vítovská D, Krasny L, Koval T, Dohnalek J, Ziemska-Legi Cka J, Grynberg M, Jarnot P, Gruca A, Jensen MR, Blackledge M, Zidek L
RgGuinier 4.5 nm
Dmax 21.0 nm
VolumePorod 74 nm3

SASDFD8 – Histidine-binding periplasmic protein (HisBP), apo-form

UniProt ID: P0AEU0 (23-260) Histidine-binding periplasmic protein
Histidine-binding periplasmic protein experimental SAS data
Histidine-binding periplasmic protein Kratky plot
Sample: Histidine-binding periplasmic protein monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.0 nm
Dmax 6.0 nm
VolumePorod 32 nm3

SASDFE8 – Histidine-binding periplasmic protein (HisBP) in the presence of histidine - His-bound 5-fold excess

UniProt ID: P0AEU0 (23-260) Histidine-binding periplasmic protein
Histidine-binding periplasmic protein experimental SAS data
Histidine-binding periplasmic protein Kratky plot
Sample: Histidine-binding periplasmic protein monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 1.8 nm
Dmax 5.7 nm
VolumePorod 33 nm3

SASDFF8 – Glutamine-binding periplasmic protein with hexahistidine tag (GlnBP), apo-form

UniProt ID: P0AEQ3 (23-248) Glutamine-binding periplasmic protein with hexahistidine tag
Glutamine-binding periplasmic protein with hexahistidine tag experimental SAS data
Glutamine-binding periplasmic protein with hexahistidine tag Kratky plot
Sample: Glutamine-binding periplasmic protein with hexahistidine tag monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.1 nm
Dmax 6.2 nm
VolumePorod 35 nm3

SASDFG8 – Glutamine-binding periplasmic protein with hexahistidine tag (GlnBP) in the presence of glutamine - Gln-bound 10-fold excess

UniProt ID: P0AEQ3 (23-248) Glutamine-binding periplasmic protein with hexahistidine tag
Glutamine-binding periplasmic protein with hexahistidine tag experimental SAS data
Glutamine-binding periplasmic protein with hexahistidine tag Kratky plot
Sample: Glutamine-binding periplasmic protein with hexahistidine tag monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.0 nm
Dmax 6.1 nm
VolumePorod 34 nm3

SASDFH8 – Glutamate/aspartate import solute-binding protein (DEBP), apo-form

UniProt ID: P37902 (28-302) Glutamate/aspartate import solute-binding protein
Glutamate/aspartate import solute-binding protein experimental SAS data
Glutamate/aspartate import solute-binding protein Kratky plot
Sample: Glutamate/aspartate import solute-binding protein monomer, 32 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.3 nm
Dmax 8.5 nm
VolumePorod 44 nm3

SASDFJ8 – Glutamate/aspartate import solute-binding protein (DEBP) in the presence of glutamate - Glu-bound 10-fold excess

UniProt ID: P37902 (28-302) Glutamate/aspartate import solute-binding protein
Glutamate/aspartate import solute-binding protein experimental SAS data
Glutamate/aspartate import solute-binding protein Kratky plot
Sample: Glutamate/aspartate import solute-binding protein monomer, 32 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.1 nm
Dmax 6.4 nm
VolumePorod 39 nm3

SASDFK8 – GON7, the fifth subunit of human KEOPS

UniProt ID: Q9BXV9 (2-100) EKC/KEOPS complex subunit GON7
EKC/KEOPS complex subunit GON7 experimental SAS data
EKC/KEOPS complex subunit GON7 Kratky plot
Sample: EKC/KEOPS complex subunit GON7 monomer, 13 kDa Homo sapiens protein
Buffer: 20 mM MES, 200 mM NaCl, 5 mM β-mercaptoethanol, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Mar 26
Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. Nat Commun 10(1):3967 (2019)
Arrondel C, Missoury S, Snoek R, Patat J, Menara G, Collinet B, Liger D, Durand D, Gribouval O, Boyer O, Buscara L, Martin G, Machuca E, Nevo F, Lescop E, Braun DA, Boschat AC, Sanquer S, Guerrera IC, Revy P, Parisot M, Masson C, Boddaert N, Charbit M, Decramer S, Novo R, Macher MA, Ranchin B, Bacchetta J, Laurent A, Collardeau-Frachon S, van Eerde AM, Hildebrandt F, Magen D, Antignac C, van Tilbeurgh H, Mollet G
RgGuinier 3.1 nm
Dmax 12.5 nm
VolumePorod 46 nm3

SASDFL8 – GON7, the fifth subunit of human KEOPS, bound to LAGE3-OSGEP (EKC/KEOPS complex subunit:Probable tRNA N6-adenosine threonylcarbamoyltransferase)

UniProt ID: Q9BXV9 (1-100) EKC/KEOPS complex subunit GON7

UniProt ID: Q14657 (1-143) EKC/KEOPS complex subunit LAGE3

UniProt ID: Q9NPF4 (1-335) Probable tRNA N6-adenosine threonylcarbamoyltransferase
EKC/KEOPS complex subunit GON7EKC/KEOPS complex subunit LAGE3Probable tRNA N6-adenosine threonylcarbamoyltransferase experimental SAS data
OTHER model
Sample: EKC/KEOPS complex subunit GON7 monomer, 12 kDa Homo sapiens protein
EKC/KEOPS complex subunit LAGE3 monomer, 15 kDa Homo sapiens protein
Probable tRNA N6-adenosine threonylcarbamoyltransferase monomer, 36 kDa Homo sapiens protein
Buffer: 20 mM MES, 200 mM NaCl, 5 mM β-mercaptoethanol, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 May 12
Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. Nat Commun 10(1):3967 (2019)
Arrondel C, Missoury S, Snoek R, Patat J, Menara G, Collinet B, Liger D, Durand D, Gribouval O, Boyer O, Buscara L, Martin G, Machuca E, Nevo F, Lescop E, Braun DA, Boschat AC, Sanquer S, Guerrera IC, Revy P, Parisot M, Masson C, Boddaert N, Charbit M, Decramer S, Novo R, Macher MA, Ranchin B, Bacchetta J, Laurent A, Collardeau-Frachon S, van Eerde AM, Hildebrandt F, Magen D, Antignac C, van Tilbeurgh H, Mollet G
RgGuinier 3.1 nm
Dmax 11.5 nm
VolumePorod 91 nm3

SASDFM8 – GON7, the fifth subunit of human KEOPS, bound to the EKC/KEOPS complex subunit, LAGE3

UniProt ID: Q9BXV9 (2-100) EKC/KEOPS complex subunit GON7

UniProt ID: Q14657 (2-143) EKC/KEOPS complex subunit LAGE3
EKC/KEOPS complex subunit GON7EKC/KEOPS complex subunit LAGE3 experimental SAS data
EKC/KEOPS complex subunit GON7 EKC/KEOPS complex subunit LAGE3 Kratky plot
Sample: EKC/KEOPS complex subunit GON7 dimer, 25 kDa Homo sapiens protein
EKC/KEOPS complex subunit LAGE3 dimer, 33 kDa Homo sapiens protein
Buffer: 20 mM MES, 200 mM NaCl, 5 mM β-mercaptoethanol, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Mar 19
Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. Nat Commun 10(1):3967 (2019)
Arrondel C, Missoury S, Snoek R, Patat J, Menara G, Collinet B, Liger D, Durand D, Gribouval O, Boyer O, Buscara L, Martin G, Machuca E, Nevo F, Lescop E, Braun DA, Boschat AC, Sanquer S, Guerrera IC, Revy P, Parisot M, Masson C, Boddaert N, Charbit M, Decramer S, Novo R, Macher MA, Ranchin B, Bacchetta J, Laurent A, Collardeau-Frachon S, van Eerde AM, Hildebrandt F, Magen D, Antignac C, van Tilbeurgh H, Mollet G
RgGuinier 3.6 nm
Dmax 15.5 nm
VolumePorod 126 nm3