Browse by MODEL: No model

SASDR28 – Human wild-type nicotinamide phosphoribosyltransferase (NAMPT) in the presence of nicotinamide

Nicotinamide phosphoribosyltransferase experimental SAS data
Nicotinamide phosphoribosyltransferase Kratky plot
Sample: Nicotinamide phosphoribosyltransferase dimer, 114 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM nicotinamide, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 20
Identification of structural determinants of nicotinamide phosphoribosyl transferase (NAMPT) activity and substrate selectivity. J Struct Biol :108004 (2023)
Houry D, Raasakka A, Ferrario E, Niere M, Bifulco E, Kursula P, Ziegler M
RgGuinier 3.2 nm
Dmax 12.8 nm
VolumePorod 166 nm3

SASDR38 – Human wild-type nicotinamide phosphoribosyltransferase (NAMPT) in the presence of nicotinic acid

Nicotinamide phosphoribosyltransferase experimental SAS data
Nicotinamide phosphoribosyltransferase Kratky plot
Sample: Nicotinamide phosphoribosyltransferase dimer, 114 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM nicotinic acid, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 20
Identification of structural determinants of nicotinamide phosphoribosyl transferase (NAMPT) activity and substrate selectivity. J Struct Biol :108004 (2023)
Houry D, Raasakka A, Ferrario E, Niere M, Bifulco E, Kursula P, Ziegler M
RgGuinier 3.3 nm
Dmax 12.9 nm
VolumePorod 180 nm3

SASDR48 – Human wild-type nicotinamide phosphoribosyltransferase (NAMPT) in the presence of phosphoribosyl pyrophosphate

Nicotinamide phosphoribosyltransferase experimental SAS data
Nicotinamide phosphoribosyltransferase Kratky plot
Sample: Nicotinamide phosphoribosyltransferase dimer, 114 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM phosphoribosyl pyrophosphate, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 20
Identification of structural determinants of nicotinamide phosphoribosyl transferase (NAMPT) activity and substrate selectivity. J Struct Biol :108004 (2023)
Houry D, Raasakka A, Ferrario E, Niere M, Bifulco E, Kursula P, Ziegler M
RgGuinier 3.3 nm
Dmax 12.9 nm
VolumePorod 173 nm3

SASDR58 – Human nicotinamide phosphoribosyltransferase Δ42-51 loop mutant (NAMPT Δ42-51)

Nicotinamide phosphoribosyltransferase Δ42-51 experimental SAS data
Nicotinamide phosphoribosyltransferase Δ42-51 Kratky plot
Sample: Nicotinamide phosphoribosyltransferase Δ42-51 dimer, 111 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 20
Identification of structural determinants of nicotinamide phosphoribosyl transferase (NAMPT) activity and substrate selectivity. J Struct Biol :108004 (2023)
Houry D, Raasakka A, Ferrario E, Niere M, Bifulco E, Kursula P, Ziegler M
RgGuinier 3.2 nm
Dmax 11.0 nm
VolumePorod 159 nm3

SASDR68 – Human nicotinamide phosphoribosyltransferase Δ42-51 loop mutant (NAMPT Δ42-51) in the presence of nicotinamide

Nicotinamide phosphoribosyltransferase Δ42-51 experimental SAS data
Nicotinamide phosphoribosyltransferase Δ42-51 Kratky plot
Sample: Nicotinamide phosphoribosyltransferase Δ42-51 dimer, 111 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM nicotinamide, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 20
Identification of structural determinants of nicotinamide phosphoribosyl transferase (NAMPT) activity and substrate selectivity. J Struct Biol :108004 (2023)
Houry D, Raasakka A, Ferrario E, Niere M, Bifulco E, Kursula P, Ziegler M
RgGuinier 3.2 nm
Dmax 10.9 nm
VolumePorod 151 nm3

SASDR78 – Human nicotinamide phosphoribosyltransferase Δ42-51 loop mutant (NAMPT Δ42-51) in the presence of nicotinic acid

Nicotinamide phosphoribosyltransferase Δ42-51 experimental SAS data
Nicotinamide phosphoribosyltransferase Δ42-51 Kratky plot
Sample: Nicotinamide phosphoribosyltransferase Δ42-51 dimer, 111 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM nicotinic acid, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 20
Identification of structural determinants of nicotinamide phosphoribosyl transferase (NAMPT) activity and substrate selectivity. J Struct Biol :108004 (2023)
Houry D, Raasakka A, Ferrario E, Niere M, Bifulco E, Kursula P, Ziegler M
RgGuinier 3.3 nm
Dmax 11.2 nm
VolumePorod 152 nm3

SASDR88 – Human nicotinamide phosphoribosyltransferase Δ42-51 loop mutant (NAMPT Δ42-51) in the presence of phosphoribosyl pyrophosphate

Nicotinamide phosphoribosyltransferase Δ42-51 experimental SAS data
Nicotinamide phosphoribosyltransferase Δ42-51 Kratky plot
Sample: Nicotinamide phosphoribosyltransferase Δ42-51 dimer, 111 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM phosphoribosyl pyrophosphate, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 20
Identification of structural determinants of nicotinamide phosphoribosyl transferase (NAMPT) activity and substrate selectivity. J Struct Biol :108004 (2023)
Houry D, Raasakka A, Ferrario E, Niere M, Bifulco E, Kursula P, Ziegler M
RgGuinier 3.2 nm
Dmax 11.4 nm
VolumePorod 154 nm3

SASDM53 – RRM1-ZnF1-RRM2 triple domains of RNA-binding protein 5 (C191G mutant)

RNA Binding Motif protein 5 (I107T, C191G) experimental SAS data
RNA Binding Motif protein 5 (I107T, C191G) Kratky plot
Sample: RNA Binding Motif protein 5 (I107T, C191G) monomer, 26 kDa Homo sapiens protein
Buffer: 20 mM MES, 400 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2017 Feb 9
Structural basis for specific RNA recognition by the alternative splicing factor RBM5. Nat Commun 14(1):4233 (2023)
Soni K, Jagtap PKA, Martínez-Lumbreras S, Bonnal S, Geerlof A, Stehle R, Simon B, Valcárcel J, Sattler M
RgGuinier 2.3 nm
Dmax 7.8 nm
VolumePorod 36 nm3

SASDQK8 – G. gallus TRPV4 N-terminal Domain, deletion mutant ∆N104

Transient receptor potential cation channel subfamily V member 4 experimental SAS data
Transient receptor potential cation channel subfamily V member 4 Kratky plot
Sample: Transient receptor potential cation channel subfamily V member 4 monomer, 32 kDa Gallus gallus protein
Buffer: 20 mM Tris, 300 mM NaCl, 10 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Mar 16
Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity Nature Communications 14(1) (2023)
Goretzki B, Wiedemann C, McCray B, Schäfer S, Jansen J, Tebbe F, Mitrovic S, Nöth J, Cabezudo A, Donohue J, Jeffries C, Steinchen W, Stengel F, Sumner C, Hummer G, Hellmich U
RgGuinier 2.8 nm
Dmax 13.0 nm
VolumePorod 49 nm3

SASDQL8 – G. gallus TRPV4 N-terminal Domain, deletion mutant ∆N120

Transient receptor potential cation channel subfamily V member 4 experimental SAS data
Transient receptor potential cation channel subfamily V member 4 Kratky plot
Sample: Transient receptor potential cation channel subfamily V member 4 monomer, 29 kDa Gallus gallus protein
Buffer: 20 mM Tris, 300 mM NaCl, 10 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Mar 16
Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity Nature Communications 14(1) (2023)
Goretzki B, Wiedemann C, McCray B, Schäfer S, Jansen J, Tebbe F, Mitrovic S, Nöth J, Cabezudo A, Donohue J, Jeffries C, Steinchen W, Stengel F, Sumner C, Hummer G, Hellmich U
RgGuinier 2.7 nm
Dmax 12.5 nm
VolumePorod 43 nm3