SASBDB entries for UniProt ID:

SASDR55 – A complex between the periplasmic domains of cholera toxin transcriptional activator ToxR and transmembrane regulatory protein ToxS bound to bile salt

UniProt ID: P15795 (201-294) Cholera toxin transcriptional activator

UniProt ID: P24003 (25-173) Transmembrane regulatory protein ToxS

UniProt ID: None (None-None) bile acid: sodium cholate hydrate
Cholera toxin transcriptional activatorTransmembrane regulatory protein ToxSbile acid: sodium cholate hydrate experimental SAS data
CUSTOM IN-HOUSE model
Sample: Cholera toxin transcriptional activator monomer, 12 kDa Vibrio cholerae serotype … protein
Transmembrane regulatory protein ToxS dimer, 37 kDa Vibrio cholerae serotype … protein
Bile acid: sodium cholate hydrate monomer, 0 kDa
Buffer: 50 mM Na2HPO4, 300 mM NaCl, 3% glycerol, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Jul 7
Vibrio cholerae's ToxRS bile sensing system. Elife 12 (2023)
Gubensäk N, Sagmeister T, Buhlheller C, Geronimo BD, Wagner GE, Petrowitsch L, Gräwert MA, Rotzinger M, Berger TMI, Schäfer J, Usón I, Reidl J, Sánchez-Murcia PA, Zangger K, Pavkov-Keller T
RgGuinier 2.4 nm
Dmax 6.6 nm
VolumePorod 60 nm3

SASDR65 – ATP-dependent RNA helicase DDX3X (amino acids 1-580)

UniProt ID: O00571 (1-580) ATP-dependent RNA helicase DDX3X (truncation; amino acids 1-580)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 1-580) experimental SAS data
ATP-dependent RNA helicase DDX3X (truncation; amino acids 1-580) Kratky plot
Sample: ATP-dependent RNA helicase DDX3X (truncation; amino acids 1-580) monomer, 67 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 10% (v/v) glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Solution structures of DEAD-box helicase DDX3X reveal the N-terminal extension binds RNA to modulate catalysis and influence conformation
Sarah Atkinson
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 116 nm3

SASDR75 – ATP-dependent RNA helicase DDX3X (amino acids 50-580)

UniProt ID: O00571 (50-580) ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580) experimental SAS data
ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580) Kratky plot
Sample: ATP-dependent RNA helicase DDX3X (truncation; amino acids 50-580) monomer, 62 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 10% (v/v) glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Solution structures of DEAD-box helicase DDX3X reveal the N-terminal extension binds RNA to modulate catalysis and influence conformation
Sarah Atkinson
RgGuinier 3.6 nm
Dmax 12.9 nm
VolumePorod 102 nm3

SASDR85 – ATP-dependent RNA helicase DDX3X (amino acids 100-580)

UniProt ID: O00571 (100-580) ATP-dependent RNA helicase DDX3X (truncation; amino acids 100-580)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 100-580) experimental SAS data
ATP-dependent RNA helicase DDX3X (truncation; amino acids 100-580) Kratky plot
Sample: ATP-dependent RNA helicase DDX3X (truncation; amino acids 100-580) monomer, 57 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 10% (v/v) glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Solution structures of DEAD-box helicase DDX3X reveal the N-terminal extension binds RNA to modulate catalysis and influence conformation
Sarah Atkinson
RgGuinier 3.4 nm
Dmax 10.4 nm
VolumePorod 88 nm3

SASDR95 – ATP-dependent RNA helicase DDX3X (amino acids 135-580)

UniProt ID: O00571 (135-580) ATP-dependent RNA helicase DDX3X (truncation; amino acids 135-580)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 135-580) experimental SAS data
DAMFILT model
Sample: ATP-dependent RNA helicase DDX3X (truncation; amino acids 135-580) monomer, 52 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 10% (v/v) glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Solution structures of DEAD-box helicase DDX3X reveal the N-terminal extension binds RNA to modulate catalysis and influence conformation
Sarah Atkinson
RgGuinier 3.1 nm
Dmax 9.2 nm
VolumePorod 77 nm3

SASDRB5 – ATP-dependent RNA helicase DDX3X (amino acids 1-580) bound to a 15 nucleotide RNA duplex

UniProt ID: O00571 (1-580) ATP-dependent RNA helicase DDX3X (truncation; amino acids 1-580)

UniProt ID: None (None-None) 15 nucleotide RNA duplex (ATP-dependent RNA helicase DDX3X binding target)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 1-580)15 nucleotide RNA duplex (ATP-dependent RNA helicase DDX3X binding target) experimental SAS data
MONSA model
Sample: ATP-dependent RNA helicase DDX3X (truncation; amino acids 1-580) monomer, 67 kDa Homo sapiens protein
15 nucleotide RNA duplex (ATP-dependent RNA helicase DDX3X binding target) dimer, 10 kDa RNA
Buffer: 20 mM Tris, 150 mM NaCl, 10% (v/v) glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Solution structures of DEAD-box helicase DDX3X reveal the N-terminal extension binds RNA to modulate catalysis and influence conformation
Sarah Atkinson
RgGuinier 3.6 nm
Dmax 11.2 nm
VolumePorod 105 nm3

SASDRC5 – ATP-dependent RNA helicase DDX3X (amino acids 135-580) bound to a 15 nucleotide RNA duplex

UniProt ID: O00571 (135-580) ATP-dependent RNA helicase DDX3X (truncation; amino acids 135-580)

UniProt ID: None (None-None) 15 nucleotide RNA duplex (ATP-dependent RNA helicase DDX3X binding target)
ATP-dependent RNA helicase DDX3X (truncation; amino acids 135-580)15 nucleotide RNA duplex (ATP-dependent RNA helicase DDX3X binding target) experimental SAS data
MONSA model
Sample: ATP-dependent RNA helicase DDX3X (truncation; amino acids 135-580) monomer, 52 kDa Homo sapiens protein
15 nucleotide RNA duplex (ATP-dependent RNA helicase DDX3X binding target) dimer, 10 kDa RNA
Buffer: 20 mM Tris, 150 mM NaCl, 10% (v/v) glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Solution structures of DEAD-box helicase DDX3X reveal the N-terminal extension binds RNA to modulate catalysis and influence conformation
Sarah Atkinson
RgGuinier 2.9 nm
Dmax 8.5 nm

SASDRN5 – Nucleolar RNA Chaperone-Like Protein 1 (NURC1)

UniProt ID: Q9LZ65 (1-222) AT5g04600/T32M21_200
AT5g04600/T32M21_200 experimental SAS data
GASBOR model
Sample: AT5g04600/T32M21_200 monomer, 25 kDa Arabidopsis thaliana protein
Buffer: 50 mM HNa2PO4, 300 mM NaCl, 5% glycerol (v/v), 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 22
Structural and functional analysis of a plant nucleolar RNA chaperone-like protein. Sci Rep 13(1):9656 (2023)
Fernandes R, Ostendorp A, Ostendorp S, Mehrmann J, Falke S, Graewert MA, Weingartner M, Kehr J, Hoth S
RgGuinier 3.5 nm
Dmax 12.4 nm
VolumePorod 66 nm3

SASDRP5 – SEC-SAXS analysis of recombinant survival motor neuron protein (flSMN) conjugated to the protein transduction domain of HIV-1 Tat protein (Tat-flSMN)

UniProt ID: Q16637 (1-294) Survival motor neuron protein (fusion construct with the protein transduction domain of the human immunodeficiency virus type 1 Tat protein)
Survival motor neuron protein (fusion construct with the protein transduction domain of the human immunodeficiency virus type 1 Tat protein) experimental SAS data
Survival motor neuron protein (fusion construct with the protein transduction domain of the human immunodeficiency virus type 1 Tat protein) Kratky plot
Sample: Survival motor neuron protein (fusion construct with the protein transduction domain of the human immunodeficiency virus type 1 Tat protein), 533 kDa synthetic construct protein
Buffer: 50 mM Tris-HCl, 500 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Jun 13
Recombinant flSMN
Federico Forneris
RgGuinier 8.0 nm
Dmax 29.7 nm
VolumePorod 897 nm3

SASDRR5 – Like Early Starvation 1

UniProt ID: Q5EAH9 (57-578) At3g55760
At3g55760 experimental SAS data
GASBOR model
Sample: At3g55760 monomer, 60 kDa Arabidopsis thaliana protein
Buffer: 50 mM Tris, 150 mM NaCl, 10% glycerol, 2 mM DTT, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Dec 8
LIKE EARLY STARVATION 1 and EARLY STARVATION 1 promote and stabilize amylopectin phase transition in starch biosynthesis. Sci Adv 9(21):eadg7448 (2023)
Liu C, Pfister B, Osman R, Ritter M, Heutinck A, Sharma M, Eicke S, Fischer-Stettler M, Seung D, Bompard C, Abt MR, Zeeman SC
RgGuinier 3.7 nm
Dmax 16.0 nm
VolumePorod 121 nm3