The Experts below are selected from a list of 588 Experts worldwide ranked by ideXlab platform
Ping Zhang - One of the best experts on this subject based on the ideXlab platform.
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atomic resolution cryo em structure of a native like cenp a Nucleosome aided by an Antibody fragment
Nature Communications, 2019Co-Authors: Bingrui Zhou, K N S Yadav, Mario J Borgnia, Jingjun Hong, B Cao, A L Olins, D E Olins, Y Bai, Ping ZhangAbstract:Genomic DNA in eukaryotes is organized into chromatin through association with core histones to form Nucleosomes, each distinguished by their DNA sequences and histone variants. Here, we used a single-chain Antibody fragment (scFv) derived from the anti-Nucleosome Antibody mAb PL2-6 to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by the cryo-electron microscopy (cryo-EM) to 2.6 A resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A Nucleosome could only reach 3.4 A resolution. We find that scFv binds to a conserved acidic patch on the histone H2A-H2B dimer without perturbing the Nucleosome structure. Our results provide an atomic resolution cryo-EM structure of a Nucleosome and insight into the structure and function of the CENP-A Nucleosome. The scFv approach is applicable to the structural determination of other native-like Nucleosomes with distinct DNA sequences. CENP-A histone variants replace histones H3 at centromeres. Here the authors use a single-chain Antibody fragment (scFv) to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by cryo-EM to 2.6 A resolution, providing insight into the structure and function of the CENP-A Nucleosome.
Bingrui Zhou - One of the best experts on this subject based on the ideXlab platform.
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atomic resolution cryo em structure of a native like cenp a Nucleosome aided by an Antibody fragment
Nature Communications, 2019Co-Authors: Bingrui Zhou, K N S Yadav, Mario J Borgnia, Jingjun Hong, B Cao, A L Olins, D E Olins, Y Bai, Ping ZhangAbstract:Genomic DNA in eukaryotes is organized into chromatin through association with core histones to form Nucleosomes, each distinguished by their DNA sequences and histone variants. Here, we used a single-chain Antibody fragment (scFv) derived from the anti-Nucleosome Antibody mAb PL2-6 to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by the cryo-electron microscopy (cryo-EM) to 2.6 A resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A Nucleosome could only reach 3.4 A resolution. We find that scFv binds to a conserved acidic patch on the histone H2A-H2B dimer without perturbing the Nucleosome structure. Our results provide an atomic resolution cryo-EM structure of a Nucleosome and insight into the structure and function of the CENP-A Nucleosome. The scFv approach is applicable to the structural determination of other native-like Nucleosomes with distinct DNA sequences. CENP-A histone variants replace histones H3 at centromeres. Here the authors use a single-chain Antibody fragment (scFv) to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by cryo-EM to 2.6 A resolution, providing insight into the structure and function of the CENP-A Nucleosome.
Y Bai - One of the best experts on this subject based on the ideXlab platform.
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atomic resolution cryo em structure of a native like cenp a Nucleosome aided by an Antibody fragment
Nature Communications, 2019Co-Authors: Bingrui Zhou, K N S Yadav, Mario J Borgnia, Jingjun Hong, B Cao, A L Olins, D E Olins, Y Bai, Ping ZhangAbstract:Genomic DNA in eukaryotes is organized into chromatin through association with core histones to form Nucleosomes, each distinguished by their DNA sequences and histone variants. Here, we used a single-chain Antibody fragment (scFv) derived from the anti-Nucleosome Antibody mAb PL2-6 to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by the cryo-electron microscopy (cryo-EM) to 2.6 A resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A Nucleosome could only reach 3.4 A resolution. We find that scFv binds to a conserved acidic patch on the histone H2A-H2B dimer without perturbing the Nucleosome structure. Our results provide an atomic resolution cryo-EM structure of a Nucleosome and insight into the structure and function of the CENP-A Nucleosome. The scFv approach is applicable to the structural determination of other native-like Nucleosomes with distinct DNA sequences. CENP-A histone variants replace histones H3 at centromeres. Here the authors use a single-chain Antibody fragment (scFv) to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by cryo-EM to 2.6 A resolution, providing insight into the structure and function of the CENP-A Nucleosome.
D E Olins - One of the best experts on this subject based on the ideXlab platform.
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atomic resolution cryo em structure of a native like cenp a Nucleosome aided by an Antibody fragment
Nature Communications, 2019Co-Authors: Bingrui Zhou, K N S Yadav, Mario J Borgnia, Jingjun Hong, B Cao, A L Olins, D E Olins, Y Bai, Ping ZhangAbstract:Genomic DNA in eukaryotes is organized into chromatin through association with core histones to form Nucleosomes, each distinguished by their DNA sequences and histone variants. Here, we used a single-chain Antibody fragment (scFv) derived from the anti-Nucleosome Antibody mAb PL2-6 to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by the cryo-electron microscopy (cryo-EM) to 2.6 A resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A Nucleosome could only reach 3.4 A resolution. We find that scFv binds to a conserved acidic patch on the histone H2A-H2B dimer without perturbing the Nucleosome structure. Our results provide an atomic resolution cryo-EM structure of a Nucleosome and insight into the structure and function of the CENP-A Nucleosome. The scFv approach is applicable to the structural determination of other native-like Nucleosomes with distinct DNA sequences. CENP-A histone variants replace histones H3 at centromeres. Here the authors use a single-chain Antibody fragment (scFv) to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by cryo-EM to 2.6 A resolution, providing insight into the structure and function of the CENP-A Nucleosome.
A L Olins - One of the best experts on this subject based on the ideXlab platform.
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atomic resolution cryo em structure of a native like cenp a Nucleosome aided by an Antibody fragment
Nature Communications, 2019Co-Authors: Bingrui Zhou, K N S Yadav, Mario J Borgnia, Jingjun Hong, B Cao, A L Olins, D E Olins, Y Bai, Ping ZhangAbstract:Genomic DNA in eukaryotes is organized into chromatin through association with core histones to form Nucleosomes, each distinguished by their DNA sequences and histone variants. Here, we used a single-chain Antibody fragment (scFv) derived from the anti-Nucleosome Antibody mAb PL2-6 to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by the cryo-electron microscopy (cryo-EM) to 2.6 A resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A Nucleosome could only reach 3.4 A resolution. We find that scFv binds to a conserved acidic patch on the histone H2A-H2B dimer without perturbing the Nucleosome structure. Our results provide an atomic resolution cryo-EM structure of a Nucleosome and insight into the structure and function of the CENP-A Nucleosome. The scFv approach is applicable to the structural determination of other native-like Nucleosomes with distinct DNA sequences. CENP-A histone variants replace histones H3 at centromeres. Here the authors use a single-chain Antibody fragment (scFv) to stabilize human CENP-A Nucleosome containing a native α-satellite DNA and solved its structure by cryo-EM to 2.6 A resolution, providing insight into the structure and function of the CENP-A Nucleosome.
