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 …

In 2013 we established a cryo-electron microscopy (cryo-EM) technique called microcrystal
electron diffraction (MicroED). Since that time, data collection and analysis schemes have …

In the many scientific endeavors that are driven by organic chemistry, unambiguous
identification of small molecules is of paramount importance. Over the past 50 years, NMR …

A complete inventory of the forces governing protein folding is critical for productive protein
modeling, including structure prediction and de novo design, as well as understanding …

Prion diseases are caused by the misfolding of prion protein (PrP). Misfolded PrP forms
protease-resistant aggregates in vivo (PrPSc) that are able to template the conversion of the …

MyD88 and MAL are Toll-like receptor (TLR) adaptors that signal to induce pro-inflammatory
cytokine production. We previously observed that the TIR domain of MAL (MALTIR) forms …

Molecular self-assembly is pervasive in the formation of living and synthetic materials.
Knowledge gained from research into the principles of molecular self-assembly drives …

Amyloid fibrils are a pathologically and functionally relevant state of protein folding, which is
generally accessible to polypeptide chains and differs fundamentally from the globular state …

Self-templating assemblies of the human prion protein are clinically associated with
transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a …

A long-standing goal of amyloid research has been to characterize the structural basis of the
rate-determining nucleating event. However, the ephemeral nature of nucleation has made …