F. Yabukarski

Conformational Ensembles Reveal the Origins of Serine Protease Catalysis

Ensemble-function analyses provide a quantitative model for serine protease catalysis, reveal previously unknown conformational features that contribute to their catalysis, and identify a structural motif that underlie these features and has evolved in >100 different enzymes from 32 protein folds.

Refinement of Multiconformer Ensemble Models from Multi-temperature X-ray Diffraction Data

This study refines multiconformer ensemble models from multi-temperature X-ray diffraction data of Proteinase K, revealing temperature-driven conformational changes and their functional implications.

Ensemble-function relationships to evaluate catalysis in the ketosteroid isomerase oxyanion hole

The paper evaluates catalytic effects in ketosteroid isomerase by analyzing ensemble conformations and their functional implications.

Damaged goods? Evaluating the impact of X-ray damage on conformational heterogeneity in room temperature and cryo-cooled protein crystals

This study evaluates how X-ray damage affects conformational heterogeneity in protein crystals at room temperature and cryo-cooled conditions, finding that damage effects can be minimized or eliminated.

Assessment of enzyme active site positioning and tests of catalytic mechanisms through X-ray-derived conformational ensembles

This study uses X-ray crystallography to analyze enzyme active site positioning and motions, finding limited conformational changes and challenging existing catalytic mechanisms.

A Robust Method for Collecting X-ray Diffraction Data from Protein Crystals across Physiological Temperatures

This paper introduces a method for collecting high-resolution X-ray diffraction data from protein crystals at physiological temperatures, achieving high-quality data in under 5 seconds.