Michael W. Martynowycz

GROND improves electron crystallography by correcting multiple scattering, enhancing refinement accuracy and revealing hidden structural details in various materials.

This study evaluates energy filter slit widths in MicroED to improve signal-to-noise ratio and data quality for macromolecular structure determination.

The paper solves an atomic-resolution protein structure using ab initio microED from spontaneously formed nanocrystals, achieving 0.85 Å resolution and resolving individual hydrogen atoms.

This study determines the structure of MP20, a lens membrane protein, revealing its tetrameric assembly and adhesive function in forming thin junctions essential for lens transparency.

This study shows that energy filtering improves MicroED data quality, enabling sub-atomic resolution and better structure modeling of proteinase K crystals.

This study shows that MicroED can determine atomic resolution protein structures from crystals up to one micrometer thick, much thicker than previously thought possible.