%0 Journal Article
%T A frozen portrait of a warm channel.
%A Boonen B
%A Voets T
%J Cell Calcium
%V 123
%N 0
%D 2024 Jun 28
%M 38959762
%F 4.69
%R 10.1016/j.ceca.2024.102927
%X In order to understand protein function, the field of structural biology makes extensive use of cryogenic electron microscopy (cryo-EM), a technique that enables structure determination at atomic resolution following embedding of protein particles in vitreous ice. Considering the profound effects of temperature on macromolecule function, an important-but often neglected-question is how the frozen particles relate to the actual protein conformations at physiological temperatures. In a recent study, Hu et al. compare structures of the cation channel TRPM4 "frozen" at 4 °C versus 37 °C, revealing how temperature critically affects the binding of activating Ca2+ ions and other channel modulators.