{Reference Type}: Journal Article
{Title}: A frozen portrait of a warm channel.
{Author}: Boonen B;Voets T;
{Journal}: Cell Calcium
{Volume}: 123
{Issue}: 0
{Year}: 2024 Jun 28
{Factor}: 4.69
{DOI}: 10.1016/j.ceca.2024.102927
{Abstract}: 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.