Nanocrystalline protein domains via salting-out.

Daniel G Greene, Shannon Modla, Stanley I Sandler, Norman J Wagner, Abraham M Lenhoff

Abstract read

In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

Finding order in chaos - nanocrystals in amorphous protein gels.Acta crystallographica. Section F, Structural biology communications · 2021
Article

4 · The record

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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

5 authors.

Daniel G GreeneDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716, USA.ORCID 0000-0003-1580-4805

Shannon ModlaDelaware Biotechnology Institute, Newark, DE 19713, USA.ORCID 0000-0002-8475-3960

Stanley I SandlerDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716, USA.

Norman J WagnerDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716, USA.ORCID 0000-0001-9565-619X

Abraham M LenhoffDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716, USA.ORCID 0000-0002-7831-219X

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018

$15.5M

NIGMS NIH HHS P41 GM103485

6 · The paper itself

Abstract

Protein salting-out is a well established phenomenon that in many cases leads to amorphous structures and protein gels, which are usually not considered to be useful for protein structure determination. Here, microstructural measurements of several different salted-out protein dense phases are reported, including of lysozyme, ribonuclease A and an IgG1, showing that salted-out protein gels unexpectedly contain highly ordered protein nanostructures that assemble hierarchically to create the gel. The nanocrystalline domains are approximately 10-100 nm in size, are shown to have structures commensurate with those of bulk crystals and grow on time scales in the order of an hour to a day. Beyond revealing the rich, hierarchical nanoscale to mesoscale structure of protein gels, the nanocrystals that these phases contain are candidates for structural biology on next-generation X-ray free-electron lasers, which may enable the study of biological macromolecules that are difficult or impossible to crystallize in bulk.

Indexed as

ProteinsCrystallizationCrystallography, X-RayGelsProtein DomainsGelsProteinsprotein crystallizationsalting-outsmall-angle scatteringX-ray free-electron lasers

Identifiers

PMID34726180

DOI10.1107/S2053230X21009961

PMCPMC8561819

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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.