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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
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Cryo-EM structure of human hexameric MCM2-7 complex.

Naining Xu1,2, Qingpeng Lin3, Honglei Tian2

  • 1Department of Oral and Maxillofacial Surgery, Stomatological Center, Peking University Shenzhen Hospital, Shenzhen Peking University-The Hong Kong University of Science and Technology Medical Center, Shenzhen 518036, China.

Iscience
|September 19, 2022
PubMed
Summary

Researchers revealed the cryo-EM structure of human MCM2-7, the DNA helicase core. This structure shows MCM2-7 can form double hexamers, suggesting a new mechanism for DNA replication initiation in eukaryotes.

Keywords:
Cell biologyMolecular biologyStructural biology

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • DNA replication initiation is crucial for cell division in eukaryotes.
  • The minichromosome maintenance (MCM2-7) complex forms the core of the replicative helicase.
  • Understanding MCM2-7 complex structure and function is key to DNA replication.

Purpose of the Study:

  • To determine the high-resolution cryo-electron microscopy (cryo-EM) structure of the endogenous human MCM2-7 complex.
  • To investigate the structural basis of MCM2-7 complex loading onto chromatin.
  • To elucidate novel mechanisms in eukaryotic DNA replication initiation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structure.
  • Analysis of the human MCM2-7 complex at 4.4 Å resolution.
  • Investigation of MCM2-7 self-association and potential double hexamer formation.

Main Results:

  • The cryo-EM structure of the human MCM2-7 complex was resolved at 4.4 Å.
  • The complex typically exists as an open-ring hexamer with a gap between Mcm2 and Mcm5.
  • Human MCM2-7 was observed to self-associate into a loose double hexamer structure.

Conclusions:

  • The determined structure provides critical insights into human DNA replication.
  • The observed double hexamer formation suggests a novel mechanism for MCM2-7 loading.
  • This research advances our understanding of pre-replicative complex assembly and DNA replication initiation.