Kirill Kovalev

This study investigates the structural basis of near-infrared absorption and noncanonical photoisomerization in neorhodopsin using crystallographic, spectroscopic, and theoretical methods.

EasyGrid automates cryo-EM sample preparation and quality control, improving vitrification for macromolecules and mammalian cells.

This paper introduces a method to achieve microsecond time resolution in cryo-EM using jet vitrification, enabling observation of protein dynamics with near-atomic resolution.

The paper presents cryo-EM structures of FArhodopsin and proteorhodopsin, showing no retinal binding despite conserved lysine and similar fold to retinal-binding rhodopsins, with mutations identified that prevent retinal binding.

The paper characterizes CryoRhodopsins from cold environments, revealing their dual functionality and structural adaptations to low temperatures.

The paper discovers a flavin-based fluorescent protein, LSSFbFP, with a large Stokes shift, achieved through excited state proton transfer, and validates its mechanism using spectroscopy and crystallography.