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33 hits found for Kursula

SASDB52 – Death associated protein kinase (wild-type)

Death associated protein kinase wild-type experimental SAS data
NONE model
Sample: Death associated protein kinase wild-type , 37 kDa Homo sapiens protein
Buffer: 50 mM HEPES 250 mM NaCl 5mM CaCl2 0.25 mM TCEP 5% (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 18
Death-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites. Structure 24(6):851-61 (2016)
...Kursula P, Schultz C, McCarthy AA, Hart DJ, Wilmanns M
RgGuinier 2.7 nm
Dmax 8.1 nm
VolumePorod 101 nm3

SASDB62 – Death associated protein kinase (D220K mutant)

Death associated protein kinase (D220K mutant) experimental SAS data
NONE model
Sample: Death associated protein kinase (D220K mutant) , 37 kDa Homo sapiens protein
Buffer: 50 mM HEPES 250 mM NaCl 5mM CaCl2 0.25 mM TCEP 5% (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 18
Death-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites. Structure 24(6):851-61 (2016)
...Kursula P, Schultz C, McCarthy AA, Hart DJ, Wilmanns M
RgGuinier 2.5 nm
Dmax 9.0 nm
VolumePorod 89 nm3

SASDB72 – Death associated protein kinase (Basic Loop mutant)

Death associated protein kinase (Basic Loop mutant) experimental SAS data
NONE model
Sample: Death associated protein kinase (Basic Loop mutant) , 37 kDa Homo sapiens protein
Buffer: 50 mM HEPES 250 mM NaCl 5mM CaCl2 0.25 mM TCEP 5% (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 18
Death-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites. Structure 24(6):851-61 (2016)
...Kursula P, Schultz C, McCarthy AA, Hart DJ, Wilmanns M
RgGuinier 2.4 nm
Dmax 7.5 nm
VolumePorod 78 nm3

SASDAN4 – Calmodulin:peptide complex

CalmodulinC-terminal region of human myelin basic protein experimental SAS data
SASREF model
Sample: Calmodulin monomer, 17 kDa Homo sapiens protein
C-terminal region of human myelin basic protein monomer, 2 kDa Homo sapiens protein
Buffer: 25 mM Tris75 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Nov 28
Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure. BMC Struct Biol 8:10 (2008)
...Kursula P
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 36 nm3

SASDBZ4 – Tyrosine hydroxylase (Isoform 1, Homo sapiens)

Tyrosine hydroxylase, isoform 1 experimental SAS data
BUNCH model
Sample: Tyrosine hydroxylase, isoform 1 tetramer, 222 kDa Homo sapiens protein
Buffer: 20 mM Na-HEPES 200 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 14
Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme. Sci Rep 6:30390 (2016)
...Kursula P, Martinez A, Flydal MI
RgGuinier 4.7 nm
Dmax 20.0 nm
VolumePorod 520 nm3

SASDLA5 – Wild-type human myelin protein P2

Myelin P2 protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin P2 protein monomer, 15 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jul 22
Human myelin protein P2: from crystallography to time-lapse membrane imaging and neuropathy-associated variants. FEBS J (2021)
...Kursula P
RgGuinier 1.5 nm
Dmax 4.2 nm
VolumePorod 17 nm3

SASDLB5 – CMT mutant i50del of human myelin protein P2

Myelin P2 disease mutant I50del experimental SAS data
DAMMIN model
Sample: Myelin P2 disease mutant I50del monomer, 15 kDa protein
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jul 22
Human myelin protein P2: from crystallography to time-lapse membrane imaging and neuropathy-associated variants. FEBS J (2021)
...Kursula P
RgGuinier 1.5 nm
Dmax 4.0 nm
VolumePorod 17 nm3

SASDLC5 – CMT mutant M114T of human myelin protein P2

Human P2 M114T mutant experimental SAS data
DAMMIN model
Sample: Human P2 M114T mutant monomer, 15 kDa protein
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jul 22
Human myelin protein P2: from crystallography to time-lapse membrane imaging and neuropathy-associated variants. FEBS J (2021)
...Kursula P
RgGuinier 1.5 nm
Dmax 4.0 nm
VolumePorod 16 nm3

SASDLD5 – CMT mutant V115A of human myelin protein P2

Human P2 V115A mutant experimental SAS data
DAMMIN model
Sample: Human P2 V115A mutant monomer, 15 kDa protein
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jul 22
Human myelin protein P2: from crystallography to time-lapse membrane imaging and neuropathy-associated variants. FEBS J (2021)
...Kursula P
RgGuinier 1.5 nm
Dmax 4.0 nm
VolumePorod 17 nm3

SASDND6 – Human ganglioside-induced differentiation-associated protein 1 (GDAP1) missense mutant H123R, construct GDAP1∆302-358

Ganglioside-induced differentiation-associated protein 1 (H123R) experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1 (H123R) dimer, 70 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Oct 8
Structural insights into Charcot-Marie-Tooth disease-linked mutations in human GDAP1. FEBS Open Bio (2022)
...Kursula P
RgGuinier 3.1 nm
Dmax 9.9 nm
VolumePorod 107 nm3

SASDNE6 – Human ganglioside-induced differentiation-associated protein 1 (GDAP1) missense mutant R120W, construct GDAP1∆302-358

Ganglioside-induced differentiation-associated protein 1 (R120W) experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1 (R120W) dimer, 70 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jul 1
Structural insights into Charcot-Marie-Tooth disease-linked mutations in human GDAP1. FEBS Open Bio (2022)
...Kursula P
RgGuinier 3.1 nm
Dmax 10.0 nm
VolumePorod 105 nm3

SASDJR7 – Mouse cysteine sulphinic acid decarboxylase (CSAD)

Cysteine sulfinic acid decarboxylase experimental SAS data
SREFLEX model
Sample: Cysteine sulfinic acid decarboxylase dimer, 117 kDa Mus musculus protein
Buffer: 20 mM HEPES, 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Feb 4
Structure and substrate specificity determinants of the taurine biosynthetic enzyme cysteine sulphinic acid decarboxylase. J Struct Biol :107674 (2020)
...Kursula P
RgGuinier 3.4 nm
Dmax 15.0 nm
VolumePorod 198 nm3

SASDRZ7 – Human wild-type nicotinamide phosphoribosyltransferase (NAMPT)

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, 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)
...Kursula P, Ziegler M
RgGuinier 3.3 nm
Dmax 12.9 nm
VolumePorod 181 nm3

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)
...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)
...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)
...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)
...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)
...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)
...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)
...Kursula P, Ziegler M
RgGuinier 3.2 nm
Dmax 11.4 nm
VolumePorod 154 nm3

SASDJR8 – Dimeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 dimer, 68 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 21
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 3.1 nm
Dmax 101.6 nm
VolumePorod 111 nm3

SASDJS8 – Dimeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 with hexadecanedioic acid

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 dimer, 68 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Jul 11
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 3.1 nm
Dmax 9.2 nm
VolumePorod 112 nm3

SASDJT8 – Monomeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 monomer, 34 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 21
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 2.7 nm
Dmax 92.3 nm
VolumePorod 71 nm3

SASDJU8 – Monomeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 with hexadecanedioic acid

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358 monomer, 34 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Jul 11
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 2.5 nm
Dmax 8.9 nm
VolumePorod 63 nm3

SASDJV8 – Dimeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358 experimental SAS data
CORAL model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358 dimer, 70 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jun 28
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 3.1 nm
Dmax 9.9 nm
VolumePorod 106 nm3

SASDJW8 – Monomeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358, mutant Y29E/C88A

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358, mutant Y29E/C88A experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358, mutant Y29E/C88A monomer, 35 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jun 28
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 2.5 nm
Dmax 8.7 nm
VolumePorod 59 nm3

SASDJX8 – Dimeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 dimer, 74 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Jul 11
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 3.5 nm
Dmax 10.8 nm
VolumePorod 130 nm3

SASDJY8 – Dimeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 with hexadecanedioic acid

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 dimer, 74 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Jul 11
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 3.1 nm
Dmax 9.6 nm
VolumePorod 121 nm3

SASDJZ8 – Monomeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 monomer, 37 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Jul 11
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 2.7 nm
Dmax 9.0 nm
VolumePorod 69 nm3

SASDSZ8 – The DNA binding domain (DBD) of Hepatocyte nuclear factor 1-alpha (HNF-1A)

Hepatocyte nuclear factor 1-alpha experimental SAS data
Hepatocyte nuclear factor 1-alpha Kratky plot
Sample: Hepatocyte nuclear factor 1-alpha monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 500 mM NaCl, 1 mM TCEP,, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 25
Structural properties of the HNF-1A transactivation domain Frontiers in Molecular Biosciences 10 (2023)
...Kursula P
RgGuinier 2.7 nm
Dmax 10.2 nm
VolumePorod 22 nm3

SASDJ29 – Monomeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 with hexadecanedioic acid

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆319-358 monomer, 37 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Jul 11
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 2.5 nm
Dmax 8.6 nm
VolumePorod 65 nm3

SASDS29 – The DNA binding and transactivation domains (DBD-TAD) of Hepatocyte nuclear factor 1-alpha (HNF-1A)

Hepatocyte nuclear factor 1-alpha experimental SAS data
Hepatocyte nuclear factor 1-alpha Kratky plot
Sample: Hepatocyte nuclear factor 1-alpha monomer, 62 kDa Homo sapiens protein
Buffer: 4 mM Tris, 100 mM NaCl, 1 mM TCEP,, pH: 8.5
Experiment: SAXS data collected at CoSAXS, MAX IV on 2022 Apr 2
Structural properties of the HNF-1A transactivation domain Frontiers in Molecular Biosciences 10 (2023)
...Kursula P
RgGuinier 4.9 nm
Dmax 17.0 nm
VolumePorod 109 nm3

SASDJ39 – Monomeric human ganglioside-induced differentiation-associated protein 1-like 1, GDAP1L1

Ganglioside-induced differentiation-associated protein 1-like 1 (∆125-143 isoform) experimental SAS data
CORAL model
Sample: Ganglioside-induced differentiation-associated protein 1-like 1 (∆125-143 isoform) monomer, 44 kDa Homo sapiens protein
Buffer: 20 mM TRIS pH 7.5, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Dec 10
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
...Kursula P
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 73 nm3