EMD-8938

Single-particle
2.99 Å
EMD-8938 Deposition: 05/07/2018
Map released: 22/05/2019
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-8938

Cryo-EM structure of nucleosome in complex with a single chain antibody fragment

EMD-8938

Single-particle
2.99 Å
EMD-8938 Deposition: 05/07/2018
Map released: 22/05/2019
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
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
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
PUBMED: 31127102
DOI: doi:10.1038/s41467-019-10247-4
ISSN: 2041-1723
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.