8BQE

In situ structure of the Caulobacter crescentus S-layer

Summary for 8BQE

• Entry DOI: 10.2210/pdb8bqe/pdb
• EMDB information: 16183
• Descriptor: S-layer protein rsaA, 4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose, CALCIUM ION (3 entities in total)
• Functional Keywords: rsaa s-layer sub-tomogram averaging caulobacter, structural protein
• Biological source: Caulobacter vibrioides NA1000
• Total number of polymer chains: 6
• Total formula weight: 602737.66

Authors

von Kuegelgen, A.,Bharat, T. (deposition date: 2022-11-21, release date: 2022-12-28, Last modification date: 2024-07-24)

Primary citation

Zivanov, J.,Oton, J.,Ke, Z.,von Kugelgen, A.,Pyle, E.,Qu, K.,Morado, D.,Castano-Diez, D.,Zanetti, G.,Bharat, T.A.M.,Briggs, J.A.G.,Scheres, S.H.W.
A Bayesian approach to single-particle electron cryo-tomography in RELION-4.0.
Elife, 11:-, 2022

PubMed Abstract: We present a new approach for macromolecular structure determination from multiple particles in electron cryo-tomography (cryo-ET) data sets. Whereas existing subtomogram averaging approaches are based on 3D data models, we propose to optimise a regularised likelihood target that approximates a function of the 2D experimental images. In addition, analogous to Bayesian polishing and contrast transfer function (CTF) refinement in single-particle analysis, we describe the approaches that exploit the increased signal-to-noise ratio in the averaged structure to optimise tilt-series alignments, beam-induced motions of the particles throughout the tilt-series acquisition, defoci of the individual particles, as well as higher-order optical aberrations of the microscope. Implementation of our approaches in the open-source software package RELION aims to facilitate their general use, particularly for those researchers who are already familiar with its single-particle analysis tools. We illustrate for three applications that our approaches allow structure determination from cryo-ET data to resolutions sufficient for de novo atomic modelling.

PubMed: 36468689
DOI: 10.7554/eLife.83724

Experimental method

ELECTRON MICROSCOPY (3.5 Å)