Alastair G. Stewart

This study identifies TAM as a bacterial phospholipid transport system, revealing its structure and mechanism for lipid delivery to the outer membrane.

The paper characterizes the functional and structural properties of an ancestral F1-ATPase, revealing it was originally a 6-stepper that diversified into 3-, 6-, and 9-step forms.

This study reports the high-resolution cryo-EM structure of native human nucleosomes from HEK293 cells and provides mass spectrometry analysis of histone modifications.

The paper solves the cryo-EM structure of an axle-less F1-ATPase and shows that the complete γ subunit is important for efficient ATP binding.

The paper determines structures of conductive and non-conductive HERG selectivity filters and identifies a mechanism for rapid inactivation kinetics.

The paper presents high-resolution cryo-EM structures of E. coli F1Fo ATP synthase and describes a rotational sub-step of the Fo motor that explains how the F1 and Fo motors are coupled with minimal energy loss.