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Single-particle cryo-electron microscopy (cryo-EM) has emerged over the last two decades as a technique capable of studying the structure of challenging systems. The author of this Commentary discusses some of the major historical landmarks in cryo-EM that have led to its present success.
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.
Cryo-EM has emerged rapidly as a method for determining high-resolution structures of biological macromolecules. The author of this Commentary discusses just how much better this technology may get and how fast such developments are likely to happen.
Researchers develop an approach based on solid-state nuclear magnetic resonance (NMR) to study the structure of an intrinsically disordered protein under near-native conditions.
Functional magnetic resonance data are traditionally analyzed on a population level, but new work shows that meaningful information can be extracted from individual subjects.