Search

  
Advanced search  

21 hits found for Zhao

SASDK92 – Interferon-activable protein 204 from Mus musculus (Mouse) amino-acids 215-619

Interferon-activable protein 204 experimental SAS data
CHIMERA model
Sample: Interferon-activable protein 204 monomer, 47 kDa Mus musculus protein
Buffer: 20 mM HEPES, 100 mM KCl, pH: 7.4
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2013 Mar 14
Structural mechanism of DNA recognition by the p204 HIN domain. Nucleic Acids Res (2021)
...Zhao D, Chen F, Ma H, Smith P, Unterholzner L, Xiao TS, Jin T
RgGuinier 3.1 nm
Dmax 9.5 nm
VolumePorod 28 nm3

SASDUL2 – mRNA capping enzyme small subunit

Virus termination factor small subunit experimental SAS data
DAMFILT model
Sample: Virus termination factor small subunit monomer, 33 kDa Monkeypox virus (strain … protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 Jan 4
Structural basis of the monkeypox virus mRNA cap N7 methyltransferase complex. Emerg Microbes Infect 13(1):2369193 (2024)
...Zhao G, Ding J, Li J
RgGuinier 2.4 nm
Dmax 6.8 nm
VolumePorod 51 nm3

SASDUM2 – mRNA capping enzyme MTase

Virus termination factor small subunitmRNA-capping enzyme catalytic subunit experimental SAS data
DAMFILT model
Sample: Virus termination factor small subunit monomer, 33 kDa Monkeypox virus (strain … protein
mRNA-capping enzyme catalytic subunit monomer, 35 kDa Monkeypox virus (strain … protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 Jan 4
Structural basis of the monkeypox virus mRNA cap N7 methyltransferase complex. Emerg Microbes Infect 13(1):2369193 (2024)
...Zhao G, Ding J, Li J
RgGuinier 2.9 nm
Dmax 10.1 nm
VolumePorod 106 nm3

SASDKK3 – SEC-SAXS of Presequence Protease (PreP)

Presequence protease, mitochondrial experimental SAS data
Presequence protease, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 4
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
...Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.2 nm
Dmax 9.1 nm
VolumePorod 170 nm3

SASDKL3 – SEC-SAXS of Presequence Protease (PreP) with inhibitor MitoBloCK-60 (MB-60)

Presequence protease, mitochondrial experimental SAS data
Presequence protease, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 7
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
...Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.1 nm
Dmax 9.1 nm
VolumePorod 165 nm3

SASDKM3 – SEC-SAXS of Presequence Protease (PreP) with pre-sequence of citrate synthase (1-27)

Presequence protease, mitochondrialCitrate synthase, mitochondrial experimental SAS data
Presequence protease, mitochondrial Citrate synthase, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Citrate synthase, mitochondrial monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl , 20 mM EDTA, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Nov 4
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
...Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.1 nm
Dmax 8.7 nm
VolumePorod 165 nm3

SASDKN3 – SEC-SAXS of Presequence Protease (PreP) with Amyloid beta precursor protein (1-40)

Presequence protease, mitochondrialAmyloid-beta precursor protein experimental SAS data
Presequence protease, mitochondrial Amyloid-beta precursor protein Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Amyloid-beta precursor protein monomer, 4 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl , 20 mM EDTA, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 7
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
...Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.0 nm
Dmax 8.5 nm
VolumePorod 175 nm3

SASDPT3 – Histone-lysine N-methyltransferase multi protein complex: MLL1-WDR5-RBBP5-ASH2L

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Retinoblastoma-binding protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Retinoblastoma-binding protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 37 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 59 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM TECP, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Feb 1
DPY30 acts as an ASH2L-specific stabilizer to stimulate the enzyme activity of MLL family methyltransferases on different substrates. iScience 25(9):104948 (2022)
Zhao L, Huang N, Mencius J, Li Y, Xu Y, Zheng Y, He W, Li N, Zheng J, Zhuang M, Quan S, Chen Y
RgGuinier 5.2 nm
Dmax 18.5 nm
VolumePorod 386 nm3

SASDPU3 – Histone-lysine N-methyltransferase multi protein complex bound to protein dpy-30 homologue: MLL1-WDR5-RBBP5-ASH2L-DPY30

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Retinoblastoma-binding protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Protein dpy-30 homolog experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Retinoblastoma-binding protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Protein dpy-30 homolog Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 37 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 59 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Protein dpy-30 homolog dimer, 23 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM TECP, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Feb 1
DPY30 acts as an ASH2L-specific stabilizer to stimulate the enzyme activity of MLL family methyltransferases on different substrates. iScience 25(9):104948 (2022)
Zhao L, Huang N, Mencius J, Li Y, Xu Y, Zheng Y, He W, Li N, Zheng J, Zhuang M, Quan S, Chen Y
RgGuinier 5.4 nm
Dmax 17.5 nm
VolumePorod 411 nm3

SASDG54 – Human macrophage mannose receptor 1 protein

Macrophage mannose receptor 1 experimental SAS data
ITASSER model
Sample: Macrophage mannose receptor 1 dimer, 315 kDa Mouse myeloma cell … protein
Buffer: 50mM Hepes, 100mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Apr 15
Mannose receptor (CD206) activation in tumor-associated macrophages enhances adaptive and innate antitumor immune responses. Sci Transl Med 12(530) (2020)
...Zhao Y, Lopez H, Kozlov S, de Val N, Yates CC, Baljinnyam B, Marugan J, Rudloff U
RgGuinier 7.9 nm
Dmax 30.1 nm
VolumePorod 584 nm3

SASDQB5 – Elongation factor Tu from Mycobacterium tuberculosis

Elongation factor Tu experimental SAS data
DAMMIN model
Sample: Elongation factor Tu monomer, 44 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Jul 12
Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis. Commun Biol 5(1):1052 (2022)
...Zhao G, Li J
RgGuinier 3.5 nm
Dmax 9.0 nm
VolumePorod 94 nm3

SASDQC5 – Elongation factor Ts from Mycobacterium tuberculosis

Elongation factor Ts experimental SAS data
DAMMIN model
Sample: Elongation factor Ts monomer, 29 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Jul 12
Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis. Commun Biol 5(1):1052 (2022)
...Zhao G, Li J
RgGuinier 2.7 nm
Dmax 10.1 nm
VolumePorod 46 nm3

SASDQD5 – Elongation factor-Tu and Elongation factor-Ts complex from Mycobacterium tuberculosis

Elongation factor TuElongation factor Ts experimental SAS data
DAMMIN model
Sample: Elongation factor Tu monomer, 44 kDa Mycobacterium tuberculosis (strain … protein
Elongation factor Ts monomer, 29 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Jul 12
Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis. Commun Biol 5(1):1052 (2022)
...Zhao G, Li J
RgGuinier 3.1 nm
Dmax 11.2 nm
VolumePorod 111 nm3

SASDQE5 – Nucleoside triphosphate pyrophosphohydrolase (1–185)

Nucleoside triphosphate pyrophosphohydrolase experimental SAS data
DAMMIF model
Sample: Nucleoside triphosphate pyrophosphohydrolase dimer, 41 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2020 Dec 11
Structural analysis of the housecleaning nucleoside triphosphate pyrophosphohydrolase MazG from Mycobacterium tuberculosis Frontiers in Microbiology 14 (2023)
...Zhao G, Li J
RgGuinier 2.7 nm
Dmax 8.4 nm
VolumePorod 64 nm3

SASDQ38 – Nucleoside triphosphate pyrophosphohydrolase (full-length)

Nucleoside triphosphate pyrophosphohydrolase experimental SAS data
DAMMIF model
Sample: Nucleoside triphosphate pyrophosphohydrolase dimer, 71 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2022 Sep 4
Structural analysis of the housecleaning nucleoside triphosphate pyrophosphohydrolase MazG from Mycobacterium tuberculosis Frontiers in Microbiology 14 (2023)
...Zhao G, Li J
RgGuinier 3.4 nm
Dmax 12.2 nm
VolumePorod 121 nm3

SASDDU8 – Multidomain architecture of the estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains

Estrogen receptorERE1ERE2EstradiolhERa peptide1hERa peptide2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Estrogen receptor dimer, 85 kDa protein
ERE1 monomer, 6 kDa Homo sapiens DNA
ERE2 monomer, 6 kDa Homo sapiens DNA
Estradiol dimer, 0 kDa
hERa peptide1 monomer, 2 kDa protein
hERa peptide2 monomer, 2 kDa protein
Buffer: 10 mM CHES (pH9.5), 125 mM NaCl, 5mM KCl, 4 mM MgCl2, 50 mM arginine, 50 mM glutamate, 5 mM TCEP, 5% glycerol, 10 µm Zn acetate, 10 µM estradiol, pH: 9.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Aug 10
Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains. Nat Commun 9(1):3520 (2018)
...Zhao X, Albaqami A, Mendez D, Chen Y, Chakravarthy S, Gupta S, Ralston C, Kao HY, Chance MR, Yang S
RgGuinier 3.8 nm
Dmax 11.5 nm

SASDFT9 – Adhesion G-protein coupled receptor G6 - zfGpr126 S2 (-ss) ECR

Adhesion G-protein coupled receptor G6 S2 experimental SAS data
Adhesion G-protein coupled receptor G6 S2 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S2 monomer, 86 kDa Danio rerio protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
...Zhao M, Monk K, Araç D
RgGuinier 4.0 nm
Dmax 14.1 nm
VolumePorod 169 nm3

SASDFU9 – Adhesion G-protein coupled receptor G6 - zfGpr126 S1 (+ss) ECR

Adhesion G-protein coupled receptor G6 S1 experimental SAS data
Adhesion G-protein coupled receptor G6 S1 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S1 monomer, 89 kDa Danio rerio protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
...Zhao M, Monk K, Araç D
RgGuinier 4.2 nm
Dmax 14.8 nm
VolumePorod 191 nm3

SASDFV9 – Adhesion G-protein coupled receptor G6 - zfGpr126 S2 (-ss) D134A/F135A ECR

Adhesion G-protein coupled receptor G6 S2 D134A/F135A experimental SAS data
Adhesion G-protein coupled receptor G6 S2 D134A/F135A Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S2 D134A/F135A monomer, 86 kDa Danio rerio protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
...Zhao M, Monk K, Araç D
RgGuinier 4.3 nm
Dmax 14.8 nm
VolumePorod 181 nm3

SASDFW9 – Adhesion G-protein coupled receptor G6 - hGPR126 S2 (-ss) ECR

Adhesion G-protein coupled receptor G6 S2 experimental SAS data
Adhesion G-protein coupled receptor G6 S2 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S2 monomer, 88 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
...Zhao M, Monk K, Araç D
RgGuinier 4.4 nm
Dmax 15.7 nm
VolumePorod 199 nm3

SASDFX9 – Adhesion G-protein coupled receptor G6 - hGPR126 S1 (+ss) ECR

Adhesion G-protein coupled receptor G6 S1 experimental SAS data
Adhesion G-protein coupled receptor G6 S1 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S1 monomer, 91 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
...Zhao M, Monk K, Araç D
RgGuinier 4.9 nm
Dmax 17.1 nm
VolumePorod 213 nm3