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23 hits found for Han

SASDR32 – Human derived autoantibody mAb2G7 at pH 8.0

Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VHHuman derived autoantibody mAb2G7 light chain, mAb2G7 VL experimental SAS data
Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH Human derived autoantibody mAb2G7 light chain, mAb2G7 VL Kratky plot
Sample: Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH dimer, 103 kDa protein
Human derived autoantibody mAb2G7 light chain, mAb2G7 VL dimer, 51 kDa protein
Buffer: phosphate buffered saline, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2022 Dec 8
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis. Nat Struct Mol Biol (2024)
...hang J, Zhou Q, Chen S, Chen X, Yuan TF, Zhu S
RgGuinier 5.0 nm
Dmax 16.0 nm
VolumePorod 260 nm3

SASDR42 – Human derived autoantibody mAb5F6 at pH 8.0

Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VHHuman derived autoantibody mAb2G7 light chain, mAb2G7 VL experimental SAS data
Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH Human derived autoantibody mAb2G7 light chain, mAb2G7 VL Kratky plot
Sample: Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH dimer, 103 kDa protein
Human derived autoantibody mAb2G7 light chain, mAb2G7 VL dimer, 51 kDa protein
Buffer: phosphate buffered saline, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2022 Dec 8
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis. Nat Struct Mol Biol (2024)
...hang J, Zhou Q, Chen S, Chen X, Yuan TF, Zhu S
RgGuinier 5.0 nm
Dmax 15.8 nm
VolumePorod 252 nm3

SASDR52 – Human GluN1-GluN2A NMDA receptor at pH 8.0

Glutamate receptor ionotropic, NMDA 1Glutamate receptor ionotropic, NMDA 2A experimental SAS data
Glutamate receptor ionotropic, NMDA 1 Glutamate receptor ionotropic, NMDA 2A Kratky plot
Sample: Glutamate receptor ionotropic, NMDA 1 dimer, 193 kDa Homo sapiens protein
Glutamate receptor ionotropic, NMDA 2A dimer, 191 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 0.1% digitonin, 5 µM Cholesteryl Hemisuccinate TRIS Salt, 0.1 mM CHAPSO, 50 µM EDTA,1 mM Gly/Glu, 20 mM HEPES, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2022 Dec 8
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis. Nat Struct Mol Biol (2024)
...hang J, Zhou Q, Chen S, Chen X, Yuan TF, Zhu S
RgGuinier 6.6 nm
Dmax 20.4 nm
VolumePorod 1180 nm3

SASDR62 – Human GluN1-GluN2A NMDA receptor in complex with human derived autoantibody mAb2G7 at pH 8.0

Glutamate receptor ionotropic, NMDA 1Glutamate receptor ionotropic, NMDA 2AHuman derived autoantibody mAb2G7 heavy chain, mAb2G7 VHHuman derived autoantibody mAb2G7 light chain, mAb2G7 VL experimental SAS data
Glutamate receptor ionotropic, NMDA 1 Glutamate receptor ionotropic, NMDA 2A Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH Human derived autoantibody mAb2G7 light chain, mAb2G7 VL Kratky plot
Sample: Glutamate receptor ionotropic, NMDA 1 dimer, 193 kDa Homo sapiens protein
Glutamate receptor ionotropic, NMDA 2A dimer, 191 kDa Homo sapiens protein
Human derived autoantibody mAb2G7 heavy chain, mAb2G7 VH dimer, 103 kDa protein
Human derived autoantibody mAb2G7 light chain, mAb2G7 VL dimer, 51 kDa protein
Buffer: 150 mM NaCl, 0.1% digitonin, 5 µM Cholesteryl Hemisuccinate TRIS Salt, 0.1 mM CHAPSO, 50 µM EDTA,1 mM Gly/Glu, 20 mM HEPES, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2022 Dec 8
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis. Nat Struct Mol Biol (2024)
...hang J, Zhou Q, Chen S, Chen X, Yuan TF, Zhu S
RgGuinier 7.7 nm
Dmax 25.4 nm
VolumePorod 1260 nm3

SASDR72 – Human GluN1-GluN2A NMDA receptor in complex with human derived autoantibody mAb5F6 at pH 8.0

Glutamate receptor ionotropic, NMDA 1Glutamate receptor ionotropic, NMDA 2AHuman derived autoantibody mAb5F6 heavy chain, mAb5F6 VHHuman derived autoantibody mAb5F6 light chain, mAb5F6 VL experimental SAS data
Glutamate receptor ionotropic, NMDA 1 Glutamate receptor ionotropic, NMDA 2A Human derived autoantibody mAb5F6 heavy chain, mAb5F6 VH Human derived autoantibody mAb5F6 light chain, mAb5F6 VL Kratky plot
Sample: Glutamate receptor ionotropic, NMDA 1 dimer, 193 kDa Homo sapiens protein
Glutamate receptor ionotropic, NMDA 2A dimer, 191 kDa Homo sapiens protein
Human derived autoantibody mAb5F6 heavy chain, mAb5F6 VH dimer, 104 kDa Homo sapiens protein
Human derived autoantibody mAb5F6 light chain, mAb5F6 VL dimer, 52 kDa protein
Buffer: 150 mM NaCl, 0.1% digitonin, 5 µM Cholesteryl Hemisuccinate TRIS Salt, 0.1 mM CHAPSO, 50 µM EDTA,1 mM Gly/Glu, 20 mM HEPES, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2022 Dec 8
Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis. Nat Struct Mol Biol (2024)
...hang J, Zhou Q, Chen S, Chen X, Yuan TF, Zhu S
RgGuinier 9.9 nm
Dmax 31.7 nm
VolumePorod 2500 nm3

SASDBN2 – Human linear diubiquitin

Linear di-ubiquitin experimental SAS data
Human linear diubiquitin Rg histogram
Sample: Linear di-ubiquitin monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 5C, ...hang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
...Han S, Lee S
RgGuinier 2.1 nm
Dmax 6.6 nm
VolumePorod 20 nm3

SASDBP2 – Human linear triubiquitin

Human linear tri-ubiquitin experimental SAS data
Human linear triubiquitin Rg histogram
Sample: Human linear tri-ubiquitin monomer, 26 kDa Homo sapiens protein
Buffer: 50 mM Tris 150mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 5C, ...hang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
...Han S, Lee S
RgGuinier 2.5 nm
Dmax 8.6 nm
VolumePorod 36 nm3

SASDBQ2 – Human linear tetraubiquitin

Human linear tetra-ubiquitin experimental SAS data
Human linear tetraubiquitin Rg histogram
Sample: Human linear tetra-ubiquitin monomer, 34 kDa Homo sapiens protein
Buffer: 50 mM Tris 150mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 5C, ...hang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
...Han S, Lee S
RgGuinier 3.1 nm
Dmax 11.2 nm
VolumePorod 49 nm3

SASDNZ2 – Tetrameric state of soluble endoglin receptor

Endoglin experimental SAS data
DAMMIF model
Sample: Endoglin tetramer, 243 kDa Homo sapiens protein
Buffer: 10 mM Tris–HCl, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Oct 17
Structural and functional characterization of soluble endoglin receptor Biochemical and Biophysical Research Communications 383(4):386-391 (2009)
...Han T, Hwang H, Kim K
RgGuinier 7.6 nm
Dmax 26.0 nm
VolumePorod 434 nm3

SASDN23 – Homodimeric state of soluble endoglin receptor

Endoglin experimental SAS data
DAMMIF model
Sample: Endoglin dimer, 121 kDa Homo sapiens protein
Buffer: 10 mM Tris–HCl, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Oct 17
Structural and functional characterization of soluble endoglin receptor Biochemical and Biophysical Research Communications 383(4):386-391 (2009)
...Han T, Hwang H, Kim K
RgGuinier 4.7 nm
Dmax 17.0 nm
VolumePorod 173 nm3

SASDLJ3 – SH3 and multiple ankyrin repeat domains protein 3 (wild type)

SH3 and multiple ankyrin repeat domains protein 3 experimental SAS data
CORAL model
Sample: SH3 and multiple ankyrin repeat domains protein 3 monomer, 88 kDa Rattus norvegicus protein
Buffer: 100mM NaH2PO4, 100mM NaCl, 0.5mM DTT,, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jun 3
...HANK3 missense point mutations impact conformational fluctuations and protein turnover at synapses. Elife 10 (2021)
...Han Y, Molodenskiy D, Nia FH, Kreienkamp HJ, Svergun D, Kim E, Kostyukova AS, Kreutz MR, Mikhaylova M
RgGuinier 4.1 nm
Dmax 14.0 nm
VolumePorod 170 nm3

SASDLK3 – SH3 and multiple ankyrin repeat domains protein 3 with a point mutation (L68P)

SH3 and multiple ankyrin repeat domains protein 3 experimental SAS data
CORAL model
Sample: SH3 and multiple ankyrin repeat domains protein 3 monomer, 88 kDa Rattus norvegicus protein
Buffer: 100mM NaH2PO4, 100mM NaCl, 0.5mM DTT,, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jun 3
...HANK3 missense point mutations impact conformational fluctuations and protein turnover at synapses. Elife 10 (2021)
...Han Y, Molodenskiy D, Nia FH, Kreienkamp HJ, Svergun D, Kim E, Kostyukova AS, Kreutz MR, Mikhaylova M
RgGuinier 4.1 nm
Dmax 14.8 nm
VolumePorod 224 nm3

SASDLL3 – SH3 and multiple ankyrin repeat domains protein 3 with a point mutation (R12C)

SH3 and multiple ankyrin repeat domains protein 3 experimental SAS data
CORAL model
Sample: SH3 and multiple ankyrin repeat domains protein 3 monomer, 87 kDa Rattus norvegicus protein
Buffer: 100mM NaH2PO4, 100mM NaCl, 0.5mM DTT,, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jun 3
...HANK3 missense point mutations impact conformational fluctuations and protein turnover at synapses. Elife 10 (2021)
...Han Y, Molodenskiy D, Nia FH, Kreienkamp HJ, Svergun D, Kim E, Kostyukova AS, Kreutz MR, Mikhaylova M
RgGuinier 4.1 nm
Dmax 13.8 nm
VolumePorod 175 nm3

SASDGD4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-381)

Retinoblastoma-binding protein 5Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2 experimental SAS data
Retinoblastoma-binding protein 5 Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Kratky plot
Sample: Retinoblastoma-binding protein 5 monomer, 42 kDa Homo sapiens protein
Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res (2019)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
RgGuinier 5.7 nm
Dmax 18.6 nm
VolumePorod 360 nm3

SASDGE4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-480)

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 53 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res (2019)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
RgGuinier 5.0 nm
Dmax 15.3 nm
VolumePorod 256 nm3

SASDGF4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-480)L399A/L400A/I457A/L459A

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 53 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res (2019)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
RgGuinier 5.3 nm
Dmax 17.2 nm
VolumePorod 313 nm3

SASDGG4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-538)

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 59 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, ...hanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res (2019)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
RgGuinier 5.0 nm
Dmax 15.5 nm
VolumePorod 282 nm3

SASDK86 – wild-type TRIM72 (Tripartite motif-containing protein 72)

Tripartite motif-containing protein 72 experimental SAS data
DAMMIN model
Sample: Tripartite motif-containing protein 72 dimer, 105 kDa Mus musculus protein
Buffer: 25 mM Tris-HCl, pH 8.0, 300 mM NaCl, 1 mM TCEP, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2019 Dec 7
Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane. Nat Struct Mol Biol (2023)
...Han J, Jeong BC, Song JH, Jang SH, Jeong H, Kim BH, Ko YG, Park ZY, Lee KE, Hyun J, Song HK
RgGuinier 6.9 nm
Dmax 24.0 nm
VolumePorod 384 nm3

SASDK96 – tripartite motif-containing protein 72 (TRIM72) lacking the zinc finger RING domain (ΔRING)

Tripartite motif-containing protein 72 experimental SAS data
OTHER model
Sample: Tripartite motif-containing protein 72 dimer, 88 kDa Mus musculus protein
Buffer: 25 mM Tris-HCl, pH 8.0, 300 mM NaCl, 1 mM TCEP, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2019 Dec 7
Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane. Nat Struct Mol Biol (2023)
...Han J, Jeong BC, Song JH, Jang SH, Jeong H, Kim BH, Ko YG, Park ZY, Lee KE, Hyun J, Song HK
RgGuinier 5.1 nm
Dmax 18.7 nm
VolumePorod 142 nm3

SASDKW8 – Full-length pUL21 with C-terminal His-tag

Tegument protein UL21 experimental SAS data
Full-length pUL21 with C-terminal His-tag Rg histogram
Sample: Tegument protein UL21 monomer, 59 kDa Human alphaherpesvirus 1 … protein
Buffer: 20 mM Tris pH 8.5, 500 mM NaCl, 3% (v/v) glycerol, 1 mM DTT, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Sep 25
pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread. PLoS Pathog 17(8):e1009824 (2021)
...Han Y, Brown K, Wijesinghe KJ, Zhuang Y, Colaco S, Stoll GA, Tutt OS, Svobodova S, Svergun DI, Bryant NA, Deane JE, Firth AE, Jeffries CM, Crump CM, Graham SC
RgGuinier 4.2 nm
Dmax 18.1 nm
VolumePorod 90 nm3

SASDSM9 – Hen egg white lysozyme in 1 mol% ethylammonium nitrate

Lysozyme C experimental SAS data
Lysozyme C Kratky plot
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 1 mol% ethylammonium nitrate, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Nov 27
Scattering approaches to unravel protein solution behaviors in ionic liquids and deep eutectic solvents: From basic principles to recent developments Advances in Colloid and Interface Science :103242 (2024)
Han Q, Veríssimo N, Bryant S, Martin A, Huang Y, Pereira J, Santos-Ebinuma V, Zhai J, Bryant G, Drummond C, Greaves T
RgGuinier 1.6 nm
Dmax 6.2 nm
VolumePorod 20 nm3

SASDSN9 – Buffer over-subtracted hen egg white lysozyme in 1 mol% ethylammonium nitrate

Lysozyme C experimental SAS data
Lysozyme C Kratky plot
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 1 mol% ethylammonium nitrate, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Nov 27
Scattering approaches to unravel protein solution behaviors in ionic liquids and deep eutectic solvents: From basic principles to recent developments Advances in Colloid and Interface Science :103242 (2024)
Han Q, Veríssimo N, Bryant S, Martin A, Huang Y, Pereira J, Santos-Ebinuma V, Zhai J, Bryant G, Drummond C, Greaves T
RgGuinier 1.6 nm
Dmax 6.2 nm
VolumePorod 28 nm3

SASDSP9 – Buffer under-substracted hen egg white lysozyme in 1mol% ethylammonium nitrate

Lysozyme C experimental SAS data
Lysozyme C Kratky plot
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 1 mol% ethylammonium nitrate, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Nov 27
Scattering approaches to unravel protein solution behaviors in ionic liquids and deep eutectic solvents: From basic principles to recent developments Advances in Colloid and Interface Science :103242 (2024)
Han Q, Veríssimo N, Bryant S, Martin A, Huang Y, Pereira J, Santos-Ebinuma V, Zhai J, Bryant G, Drummond C, Greaves T
RgGuinier 1.6 nm
Dmax 6.2 nm
VolumePorod 23 nm3