F. Yabukarski

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.

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

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.

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

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.