Conformational heterogeneity and probability distributions from single-particle cryo-electron microscopy

WS Tang, ED Zhong, SM Hanson, EH Thiede… - Current Opinion in …, 2023 - Elsevier
Single-particle cryo-electron microscopy (cryo-EM) is a technique that takes projection
images of biomolecules frozen at cryogenic temperatures. A major advantage of this …

Methods for cryo-EM single particle reconstruction of macromolecules having continuous heterogeneity

B Toader, FJ Sigworth, RR Lederman - Journal of molecular biology, 2023 - Elsevier
Macromolecules change their shape (conformation) in the process of carrying out their
functions. The imaging by cryo-electron microscopy of rapidly-frozen, individual copies of …

Integrating molecular models into CryoEM heterogeneity analysis using scalable high-resolution deep Gaussian mixture models

M Chen, B Toader, R Lederman - Journal of molecular biology, 2023 - Elsevier
Resolving the structural variability of proteins is often key to understanding the structure–
function relationship of those macromolecular machines. Single particle analysis using …

Computational biophysics meets cryo‐EM revolution in the search for the functional dynamics of biomolecular systems

MGS Costa, M Gur, JM Krieger… - Wiley Interdisciplinary …, 2024 - Wiley Online Library
There is a variety of experimental and computational techniques available to explore protein
dynamics, each presenting advantages and limitations. One promising experimental …

Towards interpretable Cryo-EM: disentangling latent spaces of molecular conformations

DA Klindt, A Hyvärinen, A Levy, N Miolane… - Frontiers in Molecular …, 2024 - frontiersin.org
Molecules are essential building blocks of life and their different conformations (ie, shapes)
crucially determine the functional role that they play in living organisms. Cryogenic Electron …

CryoSTAR: leveraging structural priors and constraints for cryo-EM heterogeneous reconstruction

Y Li, Y Zhou, J Yuan, F Ye, Q Gu - Nature Methods, 2024 - nature.com
Resolving conformational heterogeneity in cryogenic electron microscopy datasets remains
an important challenge in structural biology. Previous methods have often been restricted to …

Revealing biomolecular structure and motion with neural ab initio cryo-EM reconstruction

A Levy, M Grzadkowski, F Poitevin, F Vallese… - bioRxiv, 2024 - biorxiv.org
Proteins and other biomolecules form dynamic macromolecular machines that are tightly
orchestrated to move, bind, and perform chemistry. Cryo-electron microscopy (cryo-EM) can …

Reconstructing Heterogeneous Cryo-EM Molecular Structures by Decomposing Them into Polymer Chains

B Koo, J Martel, A Peck, A Levy, F Poitevin… - arXiv preprint arXiv …, 2023 - arxiv.org
Cryogenic electron microscopy (cryo-EM) has transformed structural biology by allowing to
reconstruct 3D biomolecular structures up to near-atomic resolution. However, the 3D …

[PDF][PDF] Digital Twins for Enhanced Modeling and Control of Light Sources and Neutron Sources

A Edelen, J Thayer, F Poitevin, D Ratner, R Herbst… - 2024 - nitrd.gov
Light sources and neutron sources play a key role in understanding the fundamental
properties of complex matter at different time and length scales by capturing their structural …

Physics-informed geometric regularization of heterogeneous reconstructions in cryo-EM

V Prins, W Diepeveen, EJ Bekkers, O Öktem - ICLR 2024 Workshop on … - openreview.net
Many proteins are flexible and occur in a continuum of 3D conformations. A protein's 3D
conformation is the main determinant of its biological function, and is therefore of paramount …