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Elife. 2018 Nov 9;7. pii: e42166. doi: 10.7554/eLife.42166.

New tools for automated high-resolution cryo-EM structure determination in RELION-3.

Author information

1
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
2
Department of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm University, Stockholm, Sweden.
3
Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
4
Cryo-Electron Microscopy Service Platform, European Molecular Biology Laboratory, Heidelberg, Germany.
5
Department of Applied Physics, Swedish e-Science Research Center, KTH Royal Institute of Technology, Stockholm, Sweden.
#
Contributed equally

Abstract

Here, we describe the third major release of RELION. CPU-based vector acceleration has been added in addition to GPU support, which provides flexibility in use of resources and avoids memory limitations. Reference-free autopicking with Laplacian-of-Gaussian filtering and execution of jobs from python allows non-interactive processing during acquisition, including 2D-classification, de novo model generation and 3D-classification. Per-particle refinement of CTF parameters and correction of estimated beam tilt provides higher resolution reconstructions when particles are at different heights in the ice, and/or coma-free alignment has not been optimal. Ewald sphere curvature correction improves resolution for large particles. We illustrate these developments with publicly available data sets: together with a Bayesian approach to beam-induced motion correction it leads to resolution improvements of 0.2-0.7 Å compared to previous RELION versions.

KEYWORDS:

Cryo-EM; molecular biophysics; none; single-particle analysis; software; structural biology

PMID:
30412051
PMCID:
PMC6250425
DOI:
10.7554/eLife.42166
[Indexed for MEDLINE]
Free PMC Article

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