Evidence map›Paper›PMID 37335769›Full record

ArticleIUCrJ2023

Dynamical scattering in ice-embedded proteins in conventional and scanning transmission electron microscopy.

Max Leo Leidl, Carsten Sachse, Knut Müller-Caspary

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
2.2field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Max Leo LeidlDepartment of Chemistry and Centre for NanoScience, Ludwig-Maximilians-University Munich, Butenandtstrasse 11, 81377 Munich, Germany.ORCID 0000-0001-8896-1647
Carsten SachseErnst Ruska-Centre for Microscopy and Spectroscopy with Electrons (ER-C-3), Structural Biology, Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0002-1168-5143
Knut Müller-CasparyDepartment of Chemistry and Centre for NanoScience, Ludwig-Maximilians-University Munich, Butenandtstrasse 11, 81377 Munich, Germany.ORCID 0000-0002-2588-7993
Forschungszentrum Jülich · DE

Funding

Deutsche Forschungsgemeinschaft EXC 2089/1-390776260Helmholtz Association VH-NG-1317
6 · The paper itself

Abstract

Structure determination of biological macromolecules using cryogenic electron microscopy is based on applying the phase object (PO) assumption and the weak phase object (WPO) approximation to reconstruct the 3D potential density of the molecule. To enhance the understanding of image formation of protein complexes embedded in glass-like ice in a transmission electron microscope, this study addresses multiple scattering in tobacco mosaic virus (TMV) specimens. This includes the propagation inside the molecule while also accounting for the effect of structural noise. The atoms in biological macromolecules are light but are distributed over several nanometres. Commonly, PO and WPO approximations are used in most simulations and reconstruction models. Therefore, dynamical multislice simulations of TMV specimens embedded in glass-like ice were performed based on fully atomistic molecular-dynamics simulations. In the first part, the impact of multiple scattering is studied using different numbers of slices. In the second part, different sample thicknesses of the ice-embedded TMV are considered in terms of additional ice layers. It is found that single-slice models yield full frequency transfer up to a resolution of 2.5 Å, followed by attenuation up to 1.4 Å. Three slices are sufficient to reach an information transfer up to 1.0 Å. In the third part, ptychographic reconstructions based on scanning transmission electron microscopy (STEM) and single-slice models are compared with conventional TEM simulations. The ptychographic reconstructions do not need the deliberate introduction of aberrations, are capable of post-acquisition aberration correction and promise benefits for information transfer, especially at resolutions beyond 1.8 Å.

Indexed as

IceProteinsMicroscopy, ElectronMicroscopy, Electron, Scanning TransmissionIceProteinsamorphous icecryogenic electron microscopydynamical scatteringimage simulationsintegrative structural biologymolecular dynamics

Identifiers

PMID37335769
PMCPMC10324487
OpenAlexW4381251817

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.