Browse by MODEL: No model

SASDVK7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant)

Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) monomer, 12 kDa Homo sapiens protein
Buffer: 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Oct 8
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.1 nm
Dmax 7.2 nm
VolumePorod 20 nm3

SASDVL7 – Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2)

Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) experimental SAS data
Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) Kratky plot
Sample: Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) monomer, 13 kDa Homo sapiens / … protein
Buffer: 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Oct 8
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.0 nm
Dmax 6.4 nm
VolumePorod 16 nm3

SASDSN5 – A and C rich mixed sequence single stranded RNA in 100mM NaCl

Mixed sequence single stranded RNA, rich in A and C bases experimental SAS data
Mixed sequence single stranded RNA, rich in A and C bases Kratky plot
Sample: Mixed sequence single stranded RNA, rich in A and C bases monomer, 10 kDa synthetic construct RNA
Buffer: 100 mM NaCl, 10 mM MOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at Xenocs BioXolver L with GeniX3D, University of Copenhagen, Department of Drug Design and Pharmacology on 2022 Aug 19
Sequence-dependent conformational preferences of disordered single-stranded RNA. Cell Rep Phys Sci 5(11) (2024)
Wang T, He W, Pabit SA, Pollack L, Kirmizialtin S
RgGuinier 2.2 nm
Dmax 7.6 nm
VolumePorod 15 nm3

SASDCN8 – SAXS data of Legionella pneumophila phosphocholine hydrolase Lem3(19-570)

Phosphocholine hydrolase Lem3 experimental SAS data
Phosphocholine hydrolase Lem3 Kratky plot
Sample: Phosphocholine hydrolase Lem3 monomer, 63 kDa Legionella pneumophila subsp. … protein
Buffer: 300 mM NaCl, 2 mM 2-mercaptoethanol and 30 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Sep 20
The structural analysis of dephosphocholinase Legionella pneumophila Lem3
Wenhua Zhang
RgGuinier 3.5 nm
Dmax 12.2 nm
VolumePorod 95 nm3

SASDU72 – Cereblon-midi (CRBNmidi), an engineered Cereblon construct for crystallographic and biophysical studies, bound to Pomalidomide

Cereblon-midipomalidomide experimental SAS data
Cereblon-midi pomalidomide Kratky plot
Sample: Cereblon-midi monomer, 37 kDa protein
Pomalidomide monomer, 0 kDa synthetic construct
Buffer: 20 mM Hepes, 500 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Mar 1
Design of a Cereblon construct for crystallographic and biophysical studies of protein degraders Nature Communications 15(1) (2024)
Kroupova A, Spiteri V, Rutter Z, Furihata H, Darren D, Ramachandran S, Chakraborti S, Haubrich K, Pethe J, Gonzales D, Wijaya A, Rodriguez-Rios M, Sturbaut M, Lynch D, Farnaby W, Nakasone M, Zollman D, Ciulli A
RgGuinier 2.3 nm
Dmax 6.9 nm
VolumePorod 63 nm3

SASDU82 – Cereblon-midi (CRBNmidi), an engineered Cereblon construct for crystallographic and biophysical studies, bound to Iberdomide

Cereblon-midiIberdomide experimental SAS data
Cereblon-midi Iberdomide Kratky plot
Sample: Cereblon-midi monomer, 37 kDa protein
Iberdomide monomer, 0 kDa synthetic construct
Buffer: 20 mM Hepes, 500 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Mar 1
Design of a Cereblon construct for crystallographic and biophysical studies of protein degraders Nature Communications 15(1) (2024)
Kroupova A, Spiteri V, Rutter Z, Furihata H, Darren D, Ramachandran S, Chakraborti S, Haubrich K, Pethe J, Gonzales D, Wijaya A, Rodriguez-Rios M, Sturbaut M, Lynch D, Farnaby W, Nakasone M, Zollman D, Ciulli A
RgGuinier 2.4 nm
Dmax 7.7 nm
VolumePorod 68 nm3

SASDU92 – Cereblon-midi (CRBNmidi), an engineered Cereblon construct for crystallographic and biophysical studies, bound to Lenalidomide

Cereblon-midiLenalidomide experimental SAS data
Cereblon-midi Lenalidomide Kratky plot
Sample: Cereblon-midi monomer, 37 kDa protein
Lenalidomide monomer, 0 kDa synthetic construct
Buffer: 20 mM Hepes, 500 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Mar 1
Design of a Cereblon construct for crystallographic and biophysical studies of protein degraders Nature Communications 15(1) (2024)
Kroupova A, Spiteri V, Rutter Z, Furihata H, Darren D, Ramachandran S, Chakraborti S, Haubrich K, Pethe J, Gonzales D, Wijaya A, Rodriguez-Rios M, Sturbaut M, Lynch D, Farnaby W, Nakasone M, Zollman D, Ciulli A
RgGuinier 2.2 nm
Dmax 6.2 nm
VolumePorod 59 nm3

SASDVN6 – Cereblon-midi (CRBNmidi), an engineered Cereblon construct for crystallographic and biophysical studies, bound to Boc-VcN

Cereblon-midi experimental SAS data
Cereblon-midi Kratky plot
Sample: Cereblon-midi monomer, 37 kDa synthetic construct protein
Buffer: 20 mM HEPES, 500 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Jun 29
Design of a Cereblon construct for crystallographic and biophysical studies of protein degraders Nature Communications 15(1) (2024)
Kroupova A, Spiteri V, Rutter Z, Furihata H, Darren D, Ramachandran S, Chakraborti S, Haubrich K, Pethe J, Gonzales D, Wijaya A, Rodriguez-Rios M, Sturbaut M, Lynch D, Farnaby W, Nakasone M, Zollman D, Ciulli A
RgGuinier 2.3 nm
Dmax 9.1 nm
VolumePorod 63 nm3

SASDVP6 – Cereblon-midi (CRBNmidi), an engineered Cereblon construct for crystallographic and biophysical studies, bound to Boc-AcQ

Cereblon-midi experimental SAS data
Cereblon-midi Kratky plot
Sample: Cereblon-midi monomer, 37 kDa synthetic construct protein
Buffer: 20 mM HEPES, 500 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Jun 29
Design of a Cereblon construct for crystallographic and biophysical studies of protein degraders Nature Communications 15(1) (2024)
Kroupova A, Spiteri V, Rutter Z, Furihata H, Darren D, Ramachandran S, Chakraborti S, Haubrich K, Pethe J, Gonzales D, Wijaya A, Rodriguez-Rios M, Sturbaut M, Lynch D, Farnaby W, Nakasone M, Zollman D, Ciulli A
RgGuinier 2.4 nm
Dmax 9.6 nm
VolumePorod 62 nm3

SASDK78 – E3 ubiquitin/ISG15 ligase TRIM25, apo form (TRIM25 apo)

E3 ubiquitin/ISG15 ligase TRIM25 experimental SAS data
E3 ubiquitin/ISG15 ligase TRIM25 Kratky plot
Sample: E3 ubiquitin/ISG15 ligase TRIM25 dimer, 100 kDa Homo sapiens protein
Buffer: 20 mM MES, 75 mM NaCl, 1 mM TCEP, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 19
The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity. Nat Commun 15(1):8485 (2024)
Álvarez L, Haubrich K, Iselin L, Gillioz L, Ruscica V, Lapouge K, Augsten S, Huppertz I, Choudhury NR, Simon B, Masiewicz P, Lethier M, Cusack S, Rittinger K, Gabel F, Leitner A, Michlewski G, Hentze MW, Allain FHT, Castello A, Hennig J
RgGuinier 6.8 nm
Dmax 30.2 nm