SASDX77 – Palladin Ig3-Ig4 tandem domain with linker swapped for the shorter Ig4-Ig5 Linnker

Palladin Ig3-45Linker_Ig4 experimental SAS data
Palladin Ig3-Ig4 tandem domain with linker swapped for the shorter Ig4-Ig5 Linnker Rg histogram
Sample: Palladin Ig3-45Linker_Ig4 monomer, 22 kDa Mus musculus protein
Buffer: HEPES, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2023 Aug 29
The role of linker length and composition in actin binding and bundling by palladin. Biochem J 483(3):301-318 (2026)
Sargent RA, Bradford CW, Hughes LM, Ta NH, Limpiado MJ, Vattepu R, Beck MR
RgGuinier 2.9 nm
Dmax 10.4 nm
VolumePorod 27 nm3

SASDWE7 – EccA5-N terminal domain and EspG5 complex of Mycobacterium tuberculosis

ESX-5 secretion-associated protein EspG5ESX-5 secretion system protein EccA5 experimental SAS data
DAMFILT model
Sample: ESX-5 secretion-associated protein EspG5 monomer, 32 kDa Mycobacterium tuberculosis (strain … protein
ESX-5 secretion system protein EccA5 monomer, 31 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50 mM HEPES, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2025 Jan 28
The crystal structure of the TPR domain of the EccA5 ATPase and demonstration of its interaction with EspG5 from the mycobacterial ESX-5 pathway. FEBS Lett (2026)
Sharma VK, Vishwakarma J, Kabrambam R, Kumar S, Ramachandran R
RgGuinier 3.5 nm
Dmax 9.1 nm
VolumePorod 83 nm3

SASDPJ4 – N-terminal domain of EccA5

ESX-5 secretion system protein EccA5 experimental SAS data
DAMMIF model
Sample: ESX-5 secretion system protein EccA5 monomer, 31 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Mar 9
The crystal structure of the TPR domain of the EccA5 ATPase and demonstration of its interaction with EspG5 from the mycobacterial ESX-5 pathway. FEBS Lett (2026)
Sharma VK, Vishwakarma J, Kabrambam R, Kumar S, Ramachandran R
RgGuinier 2.6 nm
Dmax 7.8 nm
VolumePorod 57 nm3

SASDXL6 – Histone deacetylase 5 (HDAC5)

Histone deacetylase 5 experimental SAS data
Histone deacetylase 5 Kratky plot
Sample: Histone deacetylase 5 monomer, 51 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM KCl, 1 mM DTT,, pH: 7.5
Experiment: SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2024 Feb 29
In vitro characterization of the catalytic domain of human histone deacetylase 5 Scientific Reports (2026)
Mammen C, Hornung F, Anzenhofer C, Schumacher J, Reiners J, Li J, Mazzone F, Bilsing F, Kassack M, Kurz T, Smits S
RgGuinier 2.8 nm
Dmax 10.1 nm
VolumePorod 82 nm3

SASDYD4 – RNA component of mitochondrial RNA processing endoribonuclease (RMRP in 5 mM Mg2+)

RMRP experimental SAS data
DAMMIN model
Sample: RMRP monomer, 90 kDa Homo sapiens RNA
Buffer: 10 mM Bis-Tris, 100 mM NaCl, 5 mM MgCl2, pH: 6.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Mar 1
Human lncRNA RMRP interacts with DEAD-box helicases and modulates mitochondrial function. Proc Natl Acad Sci U S A 123(8):e2522583123 (2026)
Pereira HS, Luddu J, Veerareddygari GR, Sanghvi SK, Patel PB, Robinson ZE, Siddiqui MQ, Singh H, Patel TR
RgGuinier 7.1 nm
Dmax 23.0 nm
VolumePorod 316 nm3

SASDYE4 – RNA component of mitochondrial RNA processing endoribonuclease (RMRP in 20 mM Mg2+)

RMRP experimental SAS data
DAMMIN model
Sample: RMRP monomer, 91 kDa Homo sapiens RNA
Buffer: 10 mM Bis-Tris, 100 mM NaCl, 5 mM MgCl2, pH: 6.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Mar 1
Human lncRNA RMRP interacts with DEAD-box helicases and modulates mitochondrial function. Proc Natl Acad Sci U S A 123(8):e2522583123 (2026)
Pereira HS, Luddu J, Veerareddygari GR, Sanghvi SK, Patel PB, Robinson ZE, Siddiqui MQ, Singh H, Patel TR
RgGuinier 5.8 nm
Dmax 18.0 nm
VolumePorod 205 nm3

SASDXU7 – N-Myc proto-oncogene protein residues 1-69

N-myc proto-oncogene protein, residues 1-69 experimental SAS data
N-myc proto-oncogene protein, residues 1-69 Kratky plot
Sample: N-myc proto-oncogene protein, residues 1-69 monomer, 8 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Nov 28
The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A. Nat Commun (2026)
Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
RgGuinier 2.4 nm
Dmax 11.0 nm
VolumePorod 12 nm3

SASDXV7 – N-Myc proto-oncogene protein, residues 1-100

N-myc proto-oncogene protein, residues 1-100 experimental SAS data
N-myc proto-oncogene protein, residues 1-100 Kratky plot
Sample: N-myc proto-oncogene protein, residues 1-100 monomer, 11 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Nov 28
The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A. Nat Commun (2026)
Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
RgGuinier 3.0 nm
Dmax 13.0 nm
VolumePorod 22 nm3

SASDXW7 – Kinase domain of Aurora kinase A mutant C290A:C393A

Aurora kinase A mutant C290A:C393A experimental SAS data
Aurora kinase A mutant C290A:C393A Kratky plot
Sample: Aurora kinase A mutant C290A:C393A monomer, 33 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Nov 28
The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A. Nat Commun (2026)
Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
RgGuinier 2.2 nm
Dmax 9.5 nm
VolumePorod 59 nm3

SASDXX7 – N-Myc proto-oncogene residues 1-69 in complex with Aurora kinase A mutant C290A:C393A

N-myc proto-oncogene protein, residues 1-69Aurora kinase A mutant C290A:C393A experimental SAS data
N-myc proto-oncogene protein, residues 1-69 Aurora kinase A mutant C290A:C393A Kratky plot
Sample: N-myc proto-oncogene protein, residues 1-69 monomer, 8 kDa Homo sapiens protein
Aurora kinase A mutant C290A:C393A monomer, 33 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Nov 28
The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A. Nat Commun (2026)
Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
RgGuinier 2.5 nm
Dmax 10.2 nm
VolumePorod 62 nm3

5170 hits found.