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Nature Research congratulates the awardees of the 2017 Nobel Prize in Chemistry - Jacques Dubochet, Joachim Frank and Richard Henderson. Their pioneering work on the use of cryo-electron microscopy to solve high-resolution structures of biomolecules has provided unprecedented insights into the complexity of life. Here, we present a Collection of Research, Methods, Reviews and Comment pieces from Nature Research to celebrate the award.
Recent advances in cryo-electron microscopy are enabling researchers to solve protein structures at near-atomic resolutions, expanding the biological applicability of this technique. Michael Eisenstein reports.
Structural biologists are at last living the dream of visualizing macromolecules to uncover their function. But it means integrating different technologies, and that's no easy feat.
This report describes the outcomes of the Data Management Challenges in 3D Electron Microscopy workshop. Key topics discussed include data models, validation and raw-data archiving. The meeting participants agreed that the EMDataBank should take the lead in addressing these issues, and concrete action points were agreed upon that will have a substantial impact on the accessibility of three-dimensional EM data in biology and medicine.
Structures of the heat-sensitive TRPV1 ion channel have been solved using single-particle electron cryo-microscopy, representing a landmark in the use of this technique for structural biology. See Articles p.107 & p.113
G-protein-coupled receptors are biological targets for drug discovery. Developments in cryo-electron microscopy have enabled the solution of the structure of a class B receptor in complex with its signalling protein. Two biologists and a microscopist explain the exciting implications of this work. See Article p.118
An ABC protein that binds the ribosomal exit site suggests a new mechanism for direct regulation of translation in response to changing ATP levels in the cell.