Richard W. Baker

The paper investigates how CCDC32 interacts with AP-2 to regulate its assembly, revealing that CCDC32 inhibits assembly and requires membrane binding for complex formation.

This paper introduces a method using Ni-NTA lipid monolayers to improve cryo-EM grid preparation, enabling high-resolution structure determination of proteins and the nucleosome.

The paper reports the X-ray crystal structure of the N-terminal domain of Staphylococcus aureus GpsB, confirming its unique conformation and supporting its role in cell division machinery organization.

This study determines the structural mechanism of AP-3 membrane recruitment and activation through cryo-EM, revealing conformational changes driven by Arf1 binding and cargo engagement.

This study reveals structural insights into the RSC chromatin remodeling complex by showing how ARP binding induces conformational changes and enhances nucleosome remodeling.

This study shows that different positions of identical CTD repeats in budding yeast RNAPII have distinct functional roles, identified through mutational analysis and phenotypic measurements.