Dataset Information
Mouse apoferritin, Dataset B taken with CRYO ARM 300
Ontology highlight
ABSTRACT:
SUBMITTER: Koji Yonekura
PROVIDER: EMPIAR-11532 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Measurement of charges and chemical bonding in a cryo-EM structure.
Communications chemistry 20230531 1
Hydrogen bonding, bond polarity, and charges in protein molecules play critical roles in the stabilization of protein structures, as well as affecting their functions such as enzymatic catalysis, electron transfer, and ligand binding. These effects can potentially be measured in Coulomb potentials using cryogenic electron microscopy (cryo-EM). We here present charges and bond properties of hydrogen in a sub-1.2 Å resolution structure of a protein complex, apoferritin, by single-particle cryo-EM. ...[more]