Evidence map›Paper›PMID 42613839›Full record

ArticleBiophysical journal2026

Snapshots of internal protein crystal architecture at the nanoscale.

Shervin S Nia, Ambarneil Saha, Jung Cho, Z Hong Zhou, Peter Ercius, Matthew Mecklenburg

Abstract read
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In one paragraph

Article in Biophysical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Shervin S NiaDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA; California NanoSystems Institute, University of California, Los Angeles, CA, USA.
Ambarneil SahaNational Center for Electron Microscopy, Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA, USA. Electronic address: asaha2@lbl.gov.
Jung ChoCalifornia NanoSystems Institute, University of California, Los Angeles, CA, USA.
Z Hong ZhouDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA; California NanoSystems Institute, University of California, Los Angeles, CA, USA; Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, CA, USA.
Peter ErciusNational Center for Electron Microscopy, Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA, USA. Electronic address: percius@lbl.gov.
Matthew MecklenburgCalifornia NanoSystems Institute, University of California, Los Angeles, CA, USA. Electronic address: mmecklenburg@cnsi.ucla.edu.

Funding

Research Training in Cell and Molecular BiologyT32GM145388 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Jorge Torres · 2022 to 2026
$5.2M
High-Resolution CryoEM Reconstruction of Large ComplexesR01GM071940 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHOU, Z HONG · 2006 to 2025
$5.0M
NIGMS NIH HHS R01 GM071940NIGMS NIH HHS T32 GM145388
6 · The paper itself

Abstract

Macromolecular crystallography has historically inferred models of internal crystal architecture from reciprocal-space measurements of Bragg reflections. Nevertheless, direct real-space visualization of crystallographic disorder remains elusive, particularly at the nanoscale. Using a 15-nm probe, here we apply both ambient-temperature and cryogenic four-dimensional scanning transmission electron microscopy (4D-STEM) to map the topography of coherently diffracting domains (CDDs) in lysozyme and myoglobin microcrystals at length scales 100× finer than conventional X-ray and electron beams. Virtual dark-field images show that each Bragg peak arises from spatially distinct subvolumes representing smooth and continuous variations in local lattice orientation. Under sustained irradiation, protein CDDs undergo rearrangements spanning several micrometers of internal movement. Furthermore, pinpoint high-dose "impact crater" experiments reveal delocalized radiolytic damage propagating hundreds of nanometers from primary irradiation sites, behavior similar to small-molecule crystals but amplified in both rate and magnitude. Together, these results establish macromolecular microcrystals as dynamic assemblies whose internal architecture continuously reorganizes during irradiation, laying the foundation for realistic models of mosaicity directly informed by both real-space and reciprocal-space observations.

Indexed as

MuramidaseMyoglobinAnimalsCrystallizationMicroscopy, Electron, Scanning TransmissionModels, MolecularProtein DomainsMuramidaseMyoglobin

Identifiers

PMID42613839

What OpenQuestion holds

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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.