Cryogenic electron microscopy (cryo-EM) enables structure determination of
macromolecular objects and their assemblies. Although the techniques have been …

Cryo-electron microscopy (cryo-EM) of non-crystalline single particles is a biophysical
technique that can be used to determine the structure of biological macromolecules and …

Here, we describe the third major release of RELION. CPU-based vector acceleration has
been added in addition to GPU support, which provides flexibility in use of resources and …

For many years, structure determination of biological macromolecules by cryo-electron
microscopy (cryo-EM) was limited to large complexes or low-resolution models. With recent …

Recent advances in single-particle cryoelecton microscopy (cryo-EM) are enabling
generation of numerous near-atomic resolution structures for well-ordered protein …

Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Abstract Knowledge of the three-dimensional structures of proteins and other biological
macromolecules often aids understanding of how they perform complicated tasks in the cell …

Transient receptor potential (TRP) channels are sensors for a wide range of cellular and
environmental signals, but elucidating how these channels respond to physical and …

Until only a few years ago, single-particle electron cryo-microscopy (cryo-EM) was usually
not the first choice for many structural biologists due to its limited resolution in the range of …

Single-particle cryo-electron microscopy (cryo-EM) has emerged over the last two decades
as a technique capable of studying challenging systems that otherwise defy structural …