Abstract
Recent technical advances have dramatically increased the power and scope of structural biology. New developments in high-resolution cryo-electron microscopy, serial X-ray crystallography, and electron diffraction have been especially transformative. Here we highlight some of the latest advances and current challenges at the frontiers of atomic resolution methods for elucidating the structures and dynamical properties of macromolecules and their complexes.
Highlights
Atomic-level structural information brings deep insight into macromolecular mechanism and function, but successful applications of structural biology methods are often challenging
Major advances in structural biology have often come in waves, and structural biologists are witnessing a sea change in the range and power of available methods for structure determination
Its application to three-dimensional protein crystals re-emerged recently in work by Gonen[258], Abrahams[259], Yonekura[260], and many others. These efforts benefitted from several compelling aspects of electron diffraction, including the large electron scattering cross section, the shorter electron wavelength in conventional electron microscopes, and the ability of the method to adopt many of the computational developments and software tools honed for X-ray crystallography over the last several decades[261,262]
Summary
Atomic-level structural information brings deep insight into macromolecular mechanism and function, but successful applications of structural biology methods are often challenging. Its application to three-dimensional protein crystals re-emerged recently in work by Gonen[258], Abrahams[259], Yonekura[260], and many others These efforts benefitted from several compelling aspects of electron diffraction, including the large electron scattering cross section, the shorter electron wavelength (and flatter Ewald sphere) in conventional electron microscopes, and the ability of the method to adopt many of the computational developments and software tools honed for X-ray crystallography over the last several decades[261,262]. Combinations of different methods, new and old, should bring us closer to this ultimate goal
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