Yuan‐Chih Chang

This study compares low-magnification super-resolution and physical-pixel workflows in cryo-EM, showing that effectiveness depends on specimen-specific signal and sampling limitations.

This study determines the cryo-EM structure of ABCG5/G8 with ergosterol and shows that ergosterol activates the transporter more than cholesterol or CHS, with Y432 in the aromatic clamp playing a key role.

The paper reports cryo-EM structures of the human 26S proteasome bound to K11/K48-branched ubiquitin chains, revealing a multivalent recognition mechanism involving new binding sites for K11 and alternating K11-K48 linkages.