Browse by MACROMOLECULE type: protein

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

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

SASDNW9 – Glucose-regulated protein 78, nucleotide-binding domain

Endoplasmic reticulum chaperone BiP experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Endoplasmic reticulum chaperone BiP monomer, 42 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 21
Structural basis of CDNF interaction with the UPR regulator GRP78. Nat Commun 15(1):8175 (2024)
Graewert MA, Volkova M, Jonasson K, Määttä JAE, Gräwert T, Mamidi S, Kulesskaya N, Evenäs J, Johnsson RE, Svergun D, Bhattacharjee A, Huttunen HJ
RgGuinier 2.2 nm
Dmax 6.5 nm
VolumePorod 70 nm3

SASDNX9 – Glucose-regulated protein 78 nucleotide-binding domain (GRP78-NBD) in complex with Cerebral dopamine neurotrophic factor (CDNF)

Endoplasmic reticulum chaperone BiPCerebral dopamine neurotrophic factor experimental SAS data
SREFLEX model
Sample: Endoplasmic reticulum chaperone BiP monomer, 42 kDa Homo sapiens protein
Cerebral dopamine neurotrophic factor monomer, 21 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 21
Structural basis of CDNF interaction with the UPR regulator GRP78. Nat Commun 15(1):8175 (2024)
Graewert MA, Volkova M, Jonasson K, Määttä JAE, Gräwert T, Mamidi S, Kulesskaya N, Evenäs J, Johnsson RE, Svergun D, Bhattacharjee A, Huttunen HJ
RgGuinier 2.8 nm
Dmax 10.0 nm
VolumePorod 75 nm3