Browse by DISSEMINATION: Published

SASDVL9 – Human DNA methyltransferase 3 beta DNMT3B (413-853) and DNA methyltransferase 3-like DNMT3L (178-379)

DNA methyltransferase 3-like (178-379)DNA methyltransferase 3 beta (413-853) experimental SAS data
GASBOR model
Sample: DNA methyltransferase 3-like (178-379) dimer, 47 kDa Homo sapiens protein
DNA methyltransferase 3 beta (413-853) dimer, 100 kDa Homo sapiens protein
Buffer: 20 mM Tris, 300 mM NaCl, 1 mM TCEP, 5% glycerol, pH: 8
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2022 Nov 2
Histone modification-driven structural remodeling unleashes DNMT3B in DNA methylation. Sci Adv 11(13):eadu8116 (2025)
Cho CC, Huang HH, Jiang BC, Yang WZ, Chen YN, Yuan HS
RgGuinier 4.5 nm
Dmax 15.9 nm
VolumePorod 191 nm3

SASDVM9 – Human DNA methyltransferase 3 beta DNMT3B (413-853) and DNA methyltransferase 3-like DNMT3L (178-379) in complex with histone H3

Histone H3.3DNA methyltransferase 3-like (178-379)DNA methyltransferase 3 beta (413-853) experimental SAS data
GASBOR model
Sample: Histone H3.3 dimer, 8 kDa Homo sapiens protein
DNA methyltransferase 3-like (178-379) dimer, 47 kDa Homo sapiens protein
DNA methyltransferase 3 beta (413-853) dimer, 100 kDa Homo sapiens protein
Buffer: 20 mM Tris, 300 mM NaCl, 1 mM TCEP, 5% glycerol, pH: 8
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2022 Nov 2
Histone modification-driven structural remodeling unleashes DNMT3B in DNA methylation. Sci Adv 11(13):eadu8116 (2025)
Cho CC, Huang HH, Jiang BC, Yang WZ, Chen YN, Yuan HS
RgGuinier 4.5 nm
Dmax 16.0 nm
VolumePorod 186 nm3

SASDXF2 – Probable conserved Mce associated membrane protein (Mam1Adelta106) from M.tuberculosis

Probable conserved Mce associated membrane protein experimental SAS data
ALPHAFOLD model
Sample: Probable conserved Mce associated membrane protein tetramer, 59 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50mM Tris, 500mM NaCl, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 10
Insight into the structure and interactions of the M. tuberculosis Mce-associated membrane proteins Mam1A-1D (2025)
Hynönen M, Perumal P, Hynönen N, Doutch J, Ma K, Venkatesan R
RgGuinier 3.2 nm
Dmax 90.0 nm
VolumePorod 90 nm3

SASDXG2 – Probable conserved Mce associated membrane protein (Mam1Adelta106) from M.tuberculosis (SANS)

Probable conserved Mce associated membrane protein experimental SAS data
DAMFILT model
Sample: Probable conserved Mce associated membrane protein tetramer, 59 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50 mM Tris, 500 mM NaCl, D-C12E9, pH: 8.5
Experiment: SANS data collected at SANS2D, ISIS Neutron and Muon Source on 2019 Dec 10
Insight into the structure and interactions of the M. tuberculosis Mce-associated membrane proteins Mam1A-1D (2025)
Hynönen M, Perumal P, Hynönen N, Doutch J, Ma K, Venkatesan R
RgGuinier 2.6 nm
Dmax 8.5 nm
VolumePorod 33 nm3

SASDU23 – Heterochromatin protein HP1α, S97A mutant, full-length (HP1α_S97A) in 50 mM NaCl

Heterochromatin protein HP1α, S97A mutant, full-length experimental SAS data
Heterochromatin protein HP1α, S97A mutant, full-length Kratky plot
Sample: Heterochromatin protein HP1α, S97A mutant, full-length dimer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 50 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 Jun 2
A dynamic structural unit of phase-separated heterochromatin protein 1α as revealed by integrative structural analyses Nucleic Acids Research 53(6) (2025)
Furukawa A, Yonezawa K, Negami T, Yoshimura Y, Hayashi A, Nakayama J, Adachi N, Senda T, Shimizu K, Terada T, Shimizu N, Nishimura Y
RgGuinier 4.0 nm
Dmax 14.4 nm
VolumePorod 117 nm3

SASDU33 – Phosphorylated heterochromatin protein HP1α, S97A mutant, full-length (pHP1α_S97A) in 50 mM NaCl

phosphorylated Heterochromatin protein HP1α, S97A mutant, full-length experimental SAS data
phosphorylated Heterochromatin protein HP1α, S97A mutant, full-length Kratky plot
Sample: Phosphorylated Heterochromatin protein HP1α, S97A mutant, full-length dimer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 50 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 Jun 2
A dynamic structural unit of phase-separated heterochromatin protein 1α as revealed by integrative structural analyses Nucleic Acids Research 53(6) (2025)
Furukawa A, Yonezawa K, Negami T, Yoshimura Y, Hayashi A, Nakayama J, Adachi N, Senda T, Shimizu K, Terada T, Shimizu N, Nishimura Y
RgGuinier 3.8 nm
Dmax 19.5 nm
VolumePorod 129 nm3

SASDU43 – Heterochromatin protein HP1α, S97A mutant, full-length (HP1α_S97A) in 500 mM NaCl

Heterochromatin protein HP1α, S97A mutant, full-length experimental SAS data
Heterochromatin protein HP1α, S97A mutant, full-length Kratky plot
Sample: Heterochromatin protein HP1α, S97A mutant, full-length dimer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 500 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 Nov 19
A dynamic structural unit of phase-separated heterochromatin protein 1α as revealed by integrative structural analyses Nucleic Acids Research 53(6) (2025)
Furukawa A, Yonezawa K, Negami T, Yoshimura Y, Hayashi A, Nakayama J, Adachi N, Senda T, Shimizu K, Terada T, Shimizu N, Nishimura Y
RgGuinier 4.5 nm
Dmax 17.1 nm
VolumePorod 94 nm3

SASDU53 – Phosphorylated heterochromatin protein HP1α, S97A mutant, full-length (pHP1α_S97A) in 500 mM NaCl

phosphorylated Heterochromatin protein HP1α, S97A mutant, full-length experimental SAS data
phosphorylated Heterochromatin protein HP1α, S97A mutant, full-length Kratky plot
Sample: Phosphorylated Heterochromatin protein HP1α, S97A mutant, full-length dimer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 500 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 Nov 19
A dynamic structural unit of phase-separated heterochromatin protein 1α as revealed by integrative structural analyses Nucleic Acids Research 53(6) (2025)
Furukawa A, Yonezawa K, Negami T, Yoshimura Y, Hayashi A, Nakayama J, Adachi N, Senda T, Shimizu K, Terada T, Shimizu N, Nishimura Y
RgGuinier 4.6 nm
Dmax 17.7 nm
VolumePorod 104 nm3

SASDU63 – Heterochromatin protein HP1α, delta CSD mutant, in 50 mM NaCl

Heterochromatin protein HP1α, delta CSD mutant experimental SAS data
Heterochromatin protein HP1α, delta CSD mutant Kratky plot
Sample: Heterochromatin protein HP1α, delta CSD mutant monomer, 13 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 50 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at BL-15A2, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Nov 27
A dynamic structural unit of phase-separated heterochromatin protein 1α as revealed by integrative structural analyses Nucleic Acids Research 53(6) (2025)
Furukawa A, Yonezawa K, Negami T, Yoshimura Y, Hayashi A, Nakayama J, Adachi N, Senda T, Shimizu K, Terada T, Shimizu N, Nishimura Y
RgGuinier 2.8 nm
Dmax 13.0 nm
VolumePorod 23 nm3

SASDU73 – Phosphorylated heterochromatin protein HP1α, delta CSD mutant, in 50 mM NaCl

phosphorylated Heterochromatin protein HP1α, delta CSD mutant experimental SAS data
phosphorylated Heterochromatin protein HP1α, delta CSD mutant Kratky plot
Sample: Phosphorylated Heterochromatin protein HP1α, delta CSD mutant monomer, 13 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 50 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at BL-15A2, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Nov 27
A dynamic structural unit of phase-separated heterochromatin protein 1α as revealed by integrative structural analyses Nucleic Acids Research 53(6) (2025)
Furukawa A, Yonezawa K, Negami T, Yoshimura Y, Hayashi A, Nakayama J, Adachi N, Senda T, Shimizu K, Terada T, Shimizu N, Nishimura Y
RgGuinier 3.0 nm
Dmax 14.4 nm
VolumePorod 44 nm3