Cryo‐electron microscopy of chromatin biology

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 73; no. 6; pp. 541 - 548
• Main Authors: Wilson, Marcus D., Costa, Alessandro
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-06-2017; Wiley Subscription Services, Inc
• Subjects: Animals; Assemblies; Biochemistry; Biology; Chromatin; Chromatin - metabolism; Chromatin - ultrastructure; Cryoelectron Microscopy - methods; cryo‐electron microscopy; cryo‐EM; Deoxyribonucleic acid; DNA; Electron microscopy; Histone Code; histone modification; Humans; integrase; Models, Molecular; nucleosome; Nucleosomes; Nucleosomes - metabolism; Nucleosomes - ultrastructure; Research Papers; Reviews; Task complexity; Transmission electron microscopy; nucleosome; histone modification; chromatin; cryo-EM; integrase; cryo-electron microscopy
• ISSN: 2059-7983; 0907-4449; 2059-7983; 1399-0047
• DOI: 10.1107/S2059798317004430

The basic unit of chromatin, the nucleosome core particle (NCP), controls how DNA in eukaryotic cells is compacted, replicated and read. Since its discovery, biochemists have sought to understand how this protein–DNA complex can help to control so many diverse tasks. Recent electron‐microscopy (EM) studies on NCP‐containing assemblies have helped to describe important chromatin transactions at a molecular level. With the implementation of recent technical advances in single‐particle EM, our understanding of how nucleosomes are recognized and read looks to take a leap forward. In this review, the authors highlight recent advances in the architectural understanding of chromatin biology elucidated by EM.
This review article summarizes recent progress in our understanding of chromatin biology based on single‐particle cryo‐electron microscopy studies.