Crystallography of nanocrystalline materials has witnessed a true revolution in the past 10
years, thanks to the introduction of protocols for 3D acquisition and analysis of electron …

The ice-water interface is commonly encountered in our life, and comes into play in a wide
number of natural phenomena. Here, attention will be focused on its effects on protein …

Electron crystallography has a storied history which rivals that of its more established X-ray-
enabled counterpart. Recent advances in data collection and analysis have sparked a …

The rippled β-sheet was theorized by Pauling and Corey in 1953 as a structural motif in
which mirror image peptide strands assemble into hydrogen-bonded periodic arrays with …

Microbially-produced ice nucleating proteins (INpro) are unique molecular structures with
the highest known catalytic efficiency for ice formation. Airborne microorganisms utilize …

The rippled β-sheet is a peptidic structural motif related to but distinct from the pleated β-
sheet. Both motifs were predicted in the 1950s by Pauling and Corey. The pleated β-sheet …

Understanding crystal structures and behaviors is crucial for constructing and engineering
crystalline materials with various properties and functions. Recent advancement in three …

Diffuse scattering, observed as intensity distribution between the Bragg peaks, is associated
with deviations from the average crystal structure, generally referred to as disorder. In many …

Microcrystal electron diffraction (MicroED) is an emerging method for the structure
determination of proteins and peptides, enzyme-inhibitor complexes. Several structures of …

Assemblies of racemic β‐sheet‐forming peptides have attracted attention for biomedical
applications because racemic forms of peptides can self‐associate more avidly than do …