Evidence map›Paper›PMID 41835390›Full record

ArticlebioRxiv : the preprint server for biology2026

Modular Scaffold Crystals for Programmable Installation and Structural Observation of DNA-Binding Proteins.

Ethan T Shields, Caroline K Slaughter, Fadwa Mekkaoui, Emma N Magna, Cole Shepherd, Philip S Lukeman, Donald E Spratt, Christopher D Snow

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

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

8 authors.

Ethan T ShieldsSchool of Biomedical and Chemical Engineering, Colorado State University; Fort Collins, 80523, United States.ORCID 0000-0003-4005-5922
Caroline K SlaughterCell and Molecular Biology Program, Colorado State University; Fort Collins, 80523, United States.ORCID 0000-0002-1530-0546
Fadwa MekkaouiGustaf H. Carlson School of Chemistry and Biochemistry, Clark University; Worcester, 01610, United States.ORCID 0000-0003-4910-8154
Emma N MagnaCell and Molecular Biology Program, Colorado State University; Fort Collins, 80523, United States.ORCID 0009-0005-4061-1062
Cole ShepherdDepartment of Biochemistry, Colorado State University; Fort Collins, 80523, United States.ORCID 0009-0007-6710-847X
Philip S LukemanDepartment of Chemistry, St John's University; Queens, 11439, United States.ORCID 0000-0003-0563-5032
Donald E SprattGustaf H. Carlson School of Chemistry and Biochemistry, Clark University; Worcester, 01610, United States.ORCID 0000-0002-0699-155X
Christopher D SnowSchool of Biomedical and Chemical Engineering, Colorado State University; Fort Collins, 80523, United States.ORCID 0000-0002-7690-3519

Funding

Multiplexed imaging of viral protein processing and assembly in live cellsR01AI168459 · NIAID · COLORADO STATE UNIVERSITY · PI Christopher Davis Snow · 2022 to 2026
$2.3M
Structure and Mechanism of HERC5-dependent ISGylationR15GM126432 · NIGMS · CLARK UNIVERSITY (WORCESTER, MA) · PI SPRATT, DONALD ERIC · 2017 to 2023
$1000k
NIAID NIH HHS R01 AI168459NIGMS NIH HHS R15 GM126432
6 · The paper itself

Abstract

Inducing biomacromolecules to self-assemble into diffraction-quality crystals remains a major challenge, typically overcome by brute-force experimental screening. Inspired by Seeman's vision of DNA-junction-based scaffolds organizing guest biomacromolecules, we developed a protein-DNA co-crystal combining modular DNA programmability with robust protein-lattice diffraction. Our engineered co-crystals are composed of stacked double-stranded DNA scaffolded by protein columns, surrounding solvent channels designed to enable guest protein diffusion. DNA 'strut' variation allows positionally-controlled installation of diverse DNA binding guest proteins. Experimentally, we simply grow scaffold crystals under standardized conditions, ligate the scaffold, and soak guest proteins. Decoupling crystal growth from guest installation will enable high-throughput structure determination of diverse DNA-binding proteins and protein-macromolecule conjugates. Sub-nanometer position and orientation control of guest macromolecules will also enable functional applications beyond structural biology.

Identifiers

PMID41835390
PMCPMC12980390

What OpenQuestion holds

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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.