SASDFS3 – Murine transcription intermediary factor 1-beta, TRIM28 RBCC assembly-null mutation R184D

Transcription intermediary factor 1-beta experimental SAS data
GASBOR model
Sample: Transcription intermediary factor 1-beta dimer, 82 kDa Mus musculus protein
Buffer: 10 mM Tris 300 mM NaCl 0.1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Aug 10
A Dissection of Oligomerisation by the TRIM28 Tripartite Motif and the Interaction with Members of the Krab-ZFP Family. J Mol Biol (2019)
Sun Y, Keown JR, Black MM, Raclot C, Demarais N, Trono D, Turelli P, Goldstone DC
RgGuinier 7.0 nm
Dmax 23.2 nm
VolumePorod 232 nm3

SASDFT3 – Murine transcription intermediary factor 1-beta, TRIM28 RBCC assembly-null mutation R184D, complexed with the Krab domain of ZFP809 fused to an N-terminal MBP

Transcription intermediary factor 1-betaZinc finger protein 809 N-terminal MBP fusion experimental SAS data
GASBOR model
Sample: Transcription intermediary factor 1-beta dimer, 82 kDa Mus musculus protein
Zinc finger protein 809 N-terminal MBP fusion monomer, 52 kDa Mus musculus protein
Buffer: 10 mM Tris 300 mM NaCl 0.1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Aug 10
A Dissection of Oligomerisation by the TRIM28 Tripartite Motif and the Interaction with Members of the Krab-ZFP Family. J Mol Biol (2019)
Sun Y, Keown JR, Black MM, Raclot C, Demarais N, Trono D, Turelli P, Goldstone DC
RgGuinier 6.4 nm
Dmax 22.0 nm
VolumePorod 252 nm3

SASDFA5 – Unposphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
Resistance to inhibitors of cholinesterase 8 homolog A Kratky plot
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 51 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Apr 24
Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A. Structure (2019)
Zeng B, Mou TC, Doukov TI, Steiner A, Yu W, Papasergi-Scott M, Tall GG, Hagn F, Sprang SR
RgGuinier 3.0 nm
Dmax 10.6 nm
VolumePorod 70 nm3

SASDFB5 – Phosphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
Resistance to inhibitors of cholinesterase 8 homolog A Kratky plot
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 51 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Apr 24
Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A. Structure (2019)
Zeng B, Mou TC, Doukov TI, Steiner A, Yu W, Papasergi-Scott M, Tall GG, Hagn F, Sprang SR
RgGuinier 3.0 nm
Dmax 10.1 nm
VolumePorod 70 nm3

SASDF52 – dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE

Dosage compensation regulator experimental SAS data
dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE Rg histogram
Sample: Dosage compensation regulator monomer, 29 kDa Drosophila melanogaster protein
Buffer: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 29
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res 47(8):4319-4333 (2019)
Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 22 nm3

SASDF62 – Mixture of the dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE, and the roX2 RNA stem-loop 7 18mer-fragment, at 1.0 mg/ml

Dosage compensation regulatorroX2 stem-loop 7, 18-mer fragment experimental SAS data
Dosage compensation regulator roX2 stem-loop 7, 18-mer fragment Kratky plot
Sample: Dosage compensation regulator monomer, 29 kDa Drosophila melanogaster protein
roX2 stem-loop 7, 18-mer fragment monomer, 12 kDa synthetic construct RNA
Buffer: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 29
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res 47(8):4319-4333 (2019)
Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 3.1 nm
Dmax 13.3 nm
VolumePorod 25 nm3

SASDF72 – roX2 RNA stem-loop 7 18mer-fragment

roX2 stem-loop 7, 18-mer fragment experimental SAS data
DAMMIN model
Sample: roX2 stem-loop 7, 18-mer fragment monomer, 12 kDa synthetic construct RNA
Buffer: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 29
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res 47(8):4319-4333 (2019)
Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 1.8 nm
Dmax 8.5 nm
VolumePorod 14 nm3

SASDEF5 – Phosphoketolase (L. lactis) with 1 mM thiaminpyrophosphate and 2% v/v glycerol at pH 7.0

Probable phosphoketolase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Probable phosphoketolase dimer, 191 kDa Lactococcus lactis subsp. … protein
Buffer: 20mM potassium phosphate 150mM NaCl 0.007 %(w/v) β-octyl glucoside 1mM DTT 1mM MgCl 1mM thiaminpyrophosphate 2 %(v/v) glycerol, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 7
Crystal structure of a xylulose 5-phosphate phosphoketolase. insights into the substrate specificity for xylulose 5-phosphate. J Struct Biol (2019)
Scheidig AJ, Horvath D, Szedlacsek SE
RgGuinier 3.4 nm
Dmax 10.2 nm
VolumePorod 237 nm3

SASDEB8 – Bacillus thuringiensis LexA repressor (Bt_LexA)

Bacillus thuringiensis LexA repressor experimental SAS data
CHIMERA model
Sample: Bacillus thuringiensis LexA repressor dimer, 47 kDa Bacillus thuringiensis protein
Buffer: 20 mM Hepes, 300 mM NaCl, 10% glycerol,, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-2000, University of British Columbia on 2017 Aug 25
Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor. Structure 27(7):1094-1102.e4 (2019)
Caveney NA, Pavlin A, Caballero G, Bahun M, Hodnik V, de Castro L, Fornelos N, Butala M, Strynadka NCJ
RgGuinier 3.7 nm
VolumePorod 110 nm3

SASDEC8 – Bacillus thuringiensis LexA repressor bound to Bacteriophage pGIL01 gp7 (Bt_LexA_GIL01_gp7)

Bacillus thuringiensis LexA repressorBacteriophage pGIL01 gp7 experimental SAS data
CHIMERA model
Sample: Bacillus thuringiensis LexA repressor dimer, 47 kDa Bacillus thuringiensis protein
Bacteriophage pGIL01 gp7 tetramer, 24 kDa Bacteriophage pGIL01 protein
Buffer: 20 mM Hepes, 300 mM NaCl, 10% glycerol,, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-2000, University of British Columbia on 2017 Aug 25
Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor. Structure 27(7):1094-1102.e4 (2019)
Caveney NA, Pavlin A, Caballero G, Bahun M, Hodnik V, de Castro L, Fornelos N, Butala M, Strynadka NCJ
RgGuinier 4.4 nm

4733 hits found.