EMD-8938
Cryo-EM structure of nucleosome in complex with a single chain antibody fragment
EMD-8938
Single-particle2.99 Å
Deposition: 05/07/2018Map released: 22/05/2019
Last modified: 23/10/2024
Sample Organism:
Drosophila melanogaster,
Escherichia coli,
Mus musculus
Sample: Nucleosome-Antibody complex
Fitted models: 6dzt (Avg. Q-score: 0.589)
Deposition Authors: Yadav KNS, Zhou B-R
Sample: Nucleosome-Antibody complex
Fitted models: 6dzt (Avg. Q-score: 0.589)
Deposition Authors: Yadav KNS, Zhou B-R
Atomic resolution cryo-EM structure of a native-like CENP-A nucleosome aided by an antibody fragment.
Zhou BR 
,
Yadav KNS,
Borgnia M ,
Hong J,
Cao B,
Olins AL,
Olins DE,
Bai Y,
Zhang P
(2019) Nat Commun , 10 , 2301 - 2301
,
Yadav KNS,
Borgnia M ,
Hong J,
Cao B,
Olins AL,
Olins DE,
Bai Y,
Zhang P
(2019) Nat Commun , 10 , 2301 - 2301
Abstract:
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 Å resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A nucleosome could only reach 3.4 Å 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.
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 Å resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A nucleosome could only reach 3.4 Å 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.