Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Amyloids share a common architecture but play disparate biological roles in processes
ranging from bacterial defense mechanisms to protein misfolding diseases. Their structures …

We present a sample preparation method for cryo-electron microscopy (cryo-EM) that
requires only 3–20 nL of sample to prepare a cryo-EM grid, depending on the protocol used …

CryoEM has become the method of choice for determining the structure of large
macromolecular complexes in multiple conformations, at resolutions where unambiguous …

Although microscopes and image-analysis software for electron cryomicroscopy (cryo-EM)
have improved dramatically in recent years, specimen-preparation methods have lagged …

High-resolution structural information is essential to understand protein function. Protein-
structure determination needs a considerable amount of protein, which can be challenging …

Blotting times for conventional cryoEM specimen preparation complicate time-resolved
studies and lead to some specimens adopting preferred orientations or denaturing at the air …

The structural determination of natural products (NPs) can be arduous because of sample
heterogeneity. This often demands iterative purification processes and characterization of …

Electron microscopy (EM) introduced a fast and lasting change to structural and cellular
biology. However, the sample preparation is still the bottleneck in the cryogenic electron …

Abstract Cryo-Electron Microscopy (cryo-EM) has become an invaluable tool for structural
biology. Over the past decade, the advent of direct electron detectors and automated data …