@article {69687,
	title = {Structural dynamics of human ribosomes in situ reconstructed by exhaustive high-resolution template matching.},
	journal = {Mol Cell},
	year = {2024},
	month = {2024 Nov 25},
	abstract = {<p>Protein synthesis is central to life and requires the ribosome, which catalyzes the stepwise addition of amino acids to a polypeptide chain by undergoing a sequence of structural transformations. Here, we employed high-resolution template matching (HRTM) on cryoelectron microscopy (cryo-EM) images of directly cryofixed living cells to obtain a set of ribosomal configurations covering the entire elongation cycle, with each configuration occurring at its native abundance. HRTM{\textquoteright}s position and orientation precision and ability to detect small targets (\~{}300\&nbsp;kDa) made it possible to order these configurations along the reaction coordinate and to reconstruct molecular features of any configuration along the elongation cycle. Visualizing the cycle{\textquoteright}s structural dynamics by combining a sequence of \&gt;40 reconstructions into a 3D movie readily revealed component and ligand movements, some of them surprising, such as spring-like intramolecular motion, providing clues about the molecular mechanisms involved in some still mysterious steps during chain elongation.</p>
},
	issn = {1097-4164},
	doi = {10.1016/j.molcel.2024.11.003},
	author = {Rickgauer, J Peter and Choi, Heejun and Moore, Andrew S and Denk, Winfried and Lippincott-Schwartz, Jennifer}
}
