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

Background Since the introduction of what became today's standard for cryo-embedding of
biological macromolecules at native conditions more than 30 years ago, techniques and …

We describe new tools for the processing of electron cryo-microscopy (cryo-EM) images in
the fourth major release of the RELION software. In particular, we introduce VDAM, a …

Public archiving in structural biology is well established with the Protein Data Bank (PDB;
wwPDB. org) catering for atomic models and the Electron Microscopy Data Bank (EMDB; …

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 …

The serum level of iron in humans is tightly controlled by the action of the hormone hepcidin
on the iron efflux transporter ferroportin. Hepcidin regulates iron absorption and recycling by …

Single-particle cryo-electron tomography is an emerging technique capable of determining
the structure of proteins imaged within the native context of cells at molecular resolution …

Selecting particles from digital micrographs is an essential step in single-particle electron
cryomicroscopy (cryo-EM). As manual selection of complete datasets—typically comprising …

The acquisition of cryo-electron microscopy (cryo-EM) data from biological specimens must
be tightly coupled to data preprocessing to ensure the best data quality and microscope …

Cryo-electron microscopy is a popular method for the determination of protein structures;
however, identifying a sufficient number of particles for analysis can take months of manual …