SASDGE6 – G-quadruplex DNA from Hepatitis B virus (wild type)

G-quadrupex experimental SAS data
DAMFILT model
Sample: G-quadrupex monomer, 6 kDa Hepatitis B virus DNA
Buffer: 20 mM HEPES, 100 mM KCl, 1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jan 15
G-quadruplex from HBV genome
Trushar Patel
RgGuinier 1.7 nm
Dmax 4.0 nm
VolumePorod 13 nm3

SASDGF6 – G-quadruplex DNA from Hepatitis B virus (mutant)

G-quadruplex mutant experimental SAS data
DAMFILT model
Sample: G-quadruplex mutant monomer, 6 kDa Hepatitis B virus DNA
Buffer: 20 mM HEPES, 100 mM KCl, 1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jan 15
G-quadruplex from HBV genome
Trushar Patel
RgGuinier 1.7 nm
Dmax 5.5 nm
VolumePorod 11 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 ...
RgGuinier 6.8 nm
Dmax 30.2 nm

SASDK88 – E3 ubiquitin/ISG15 ligase TRIM25 bound to pre-let-7-a-1@1 RNA (TRIM25/pre-let-7)

E3 ubiquitin/ISG15 ligase TRIM25pre-let-7-a-1@1 experimental SAS data
E3 ubiquitin/ISG15 ligase TRIM25 pre-let-7-a-1@1 Kratky plot
Sample: E3 ubiquitin/ISG15 ligase TRIM25 dimer, 100 kDa Homo sapiens protein
pre-let-7-a-1@1 monomer, 9 kDa synthetic construct RNA
Buffer: 20 mM MES, 75 mM NaCl, 1 mM TCEP, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 14
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 ...
RgGuinier 5.7 nm
Dmax 19.8 nm

SASDK98 – E3 ubiquitin/ISG15 ligase TRIM25 bound to pre-let-7-a-1@1 RNA (TRIM25/pre-let-7): SEC-SAXS

E3 ubiquitin/ISG15 ligase TRIM25pre-let-7-a-1@1 experimental SAS data
E3 ubiquitin/ISG15 ligase TRIM25 pre-let-7-a-1@1 Kratky plot
Sample: E3 ubiquitin/ISG15 ligase TRIM25 dimer, 100 kDa Homo sapiens protein
pre-let-7-a-1@1 monomer, 9 kDa synthetic construct RNA
Buffer: 20 mM MES, 75 mM NaCl, 1 mM TCEP, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 4
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 ...
RgGuinier 5.7 nm
Dmax 23.0 nm

SASDKA8 – E3 ubiquitin/ISG15 ligase TRIM25 bound to lnczc3h7a_304-326 RNA (TRIM25/lnczc3h7a)

E3 ubiquitin/ISG15 ligase TRIM25lnczc3h7a_304-326 experimental SAS data
E3 ubiquitin/ISG15 ligase TRIM25 lnczc3h7a_304-326 Kratky plot
Sample: E3 ubiquitin/ISG15 ligase TRIM25 dimer, 100 kDa Homo sapiens protein
lnczc3h7a_304-326 monomer, 8 kDa Homo sapiens RNA
Buffer: 20 mM MES, 75 mM NaCl, 1 mM TCEP, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 12
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 ...
RgGuinier 5.8 nm
Dmax 16.6 nm

SASDUT7 – The tandem SH2 domains of Tyrosine-protein kinase SYK

Tyrosine-protein kinase SYK experimental SAS data
Tyrosine-protein kinase SYK Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.2 nm
Dmax 6.9 nm
VolumePorod 49 nm3

SASDUU7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound FCER1G diphospho-ITAM peptide

Tyrosine-protein kinase SYKHigh affinity immunoglobulin epsilon receptor subunit gamma experimental SAS data
Tyrosine-protein kinase SYK High affinity immunoglobulin epsilon receptor subunit gamma Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
High affinity immunoglobulin epsilon receptor subunit gamma monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 54 nm3

SASDUV7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound CD3G diphospho-ITAM peptide

Tyrosine-protein kinase SYKT-cell surface glycoprotein CD3 gamma chain experimental SAS data
Tyrosine-protein kinase SYK T-cell surface glycoprotein CD3 gamma chain Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
T-cell surface glycoprotein CD3 gamma chain monomer, 3 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 56 nm3

SASDUW7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound TYROBP diphospho-ITAM peptide

Tyrosine-protein kinase SYKTYRO protein tyrosine kinase-binding protein experimental SAS data
Tyrosine-protein kinase SYK TYRO protein tyrosine kinase-binding protein Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
TYRO protein tyrosine kinase-binding protein monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 53 nm3

4733 hits found.