A. Ourmazd

This study benchmarks four algorithms for determining biomolecular energy landscapes and identifying functionally relevant conformational paths using synthetic cryo-EM data.

The paper uses MISC to study Sulbactam inhibition of M. tuberculosis BlaC, revealing heterogeneity, cooperativity, and conformational changes in atomic detail.

The paper directly observes fast ligand binding in a biomedically relevant enzyme using MHz X-ray pulses at the European XFEL.

This paper presents single-femtosecond, atomic-resolution movies of a protein traversing a conical intersection, revealing its dynamical trajectories and key parameters.

The paper introduces a method to analyze conformational changes in biomolecules using single-particle cryo-EM data, revealing functional pathways in RyR1 that differ from discrete structure analyses.

The paper uses cryo-EM data to analyze conformational dynamics and energy landscapes of ligand binding in RyR1, revealing multiple binding routes and structural changes.