title: Processing of Structurally Heterogeneous Cryo-EM Data in RELION.
abstract: This chapter describes algorithmic advances in the RELION software, and how these are used in high-resolution cryo-electron microscopy (cryo-EM) structure determination. Since the presence of projections of different three-dimensional structures in the dataset probably represents the biggest challenge in cryo-EM data processing, special emphasis is placed on how to deal with structurally heterogeneous datasets. As such, this chapter aims to be of practical help to those who wish to use RELION in their cryo-EM structure determination efforts.
authors: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, United Kingdom. Electronic address: scheres@mrc-lmb.cam.ac.uk.
authors: S H W
authors: SH
authors: Scheres
mesh_terms: D000465:Algorithms; D001426:Bacterial Proteins / Q000648:ultrastructure; D020285:Cryoelectron Microscopy / Q000379:methods*; D004307:Dose-Response Relationship, Radiation; D004926:Escherichia coli / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted / Q000379:methods* / Q000706:statistics & numerical data; D021621:Imaging, Three-Dimensional / Q000295:instrumentation / Q000379:methods; D010963:Plasmodium falciparum / Q000648:ultrastructure; D011487:Protein Conformation; D012270:Ribosomes / Q000648:ultrastructure; D012984:Software; D001616:beta-Galactosidase / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins; D001616:beta-Galactosidase
keywords: Classification; Cryo-electron microscopy; Image processing; Maximum likelihood; Protein dynamics; RELION; Single-particle analysis; Structural heterogeneity