Evidence map›Paper›PMID 38402242›Full record

ArticleNature communications2024

A streamlined approach to structure elucidation using in cellulo crystallized recombinant proteins, InCellCryst.

Robert Schönherr, Juliane Boger, J Mia Lahey-Rudolph, Mareike Harms, Jacqueline Kaiser, Sophie Nachtschatt, Marla Wobbe, Rainer Duden, Peter König, Gleb Bourenkov and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Chemical reviews · 2026
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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

12 authors.

Robert Schönherr *Institute of Biochemistry, University of Lübeck, Lübeck, Germany.
Juliane Boger *Institute of Biochemistry, University of Lübeck, Lübeck, Germany.ORCID 0000-0003-2030-4370
J Mia Lahey-Rudolph *Institute of Biochemistry, University of Lübeck, Lübeck, Germany.ORCID 0000-0001-5279-7267
Mareike HarmsInstitute of Biochemistry, University of Lübeck, Lübeck, Germany.
Jacqueline KaiserInstitute of Biochemistry, University of Lübeck, Lübeck, Germany.ORCID 0009-0006-8058-9469
Sophie NachtschattInstitute of Biochemistry, University of Lübeck, Lübeck, Germany.ORCID 0009-0000-8144-1534
Marla WobbeInstitute of Biochemistry, University of Lübeck, Lübeck, Germany.
Rainer DudenInstitute of Biology, University of Lübeck, Lübeck, Germany.
Peter KönigInstitute of Anatomy, University of Lübeck, Lübeck, Germany.
Gleb BourenkovEuropean Molecular Biology Laboratory, Hamburg Unit c/o Deutsches Elektronen-Synchrotron DESY, Hamburg, Germany.ORCID 0000-0002-2617-5920
Thomas R SchneiderEuropean Molecular Biology Laboratory, Hamburg Unit c/o Deutsches Elektronen-Synchrotron DESY, Hamburg, Germany.ORCID 0000-0001-6955-7374
Lars RedeckeInstitute of Biochemistry, University of Lübeck, Lübeck, Germany. redecke@biochem.uni-luebeck.de.ORCID 0000-0002-5938-9431

Funding

Bundesministerium für Bildung und Forschung (Federal Ministry of Education and Research) 05K18FLADeutsche Forschungsgemeinschaft (German Research Foundation) EXC 306
6 · The paper itself

Abstract

With the advent of serial X-ray crystallography on microfocus beamlines at free-electron laser and synchrotron facilities, the demand for protein microcrystals has significantly risen in recent years. However, by in vitro crystallization extensive efforts are usually required to purify proteins and produce sufficiently homogeneous microcrystals. Here, we present InCellCryst, an advanced pipeline for producing homogeneous microcrystals directly within living insect cells. Our baculovirus-based cloning system enables the production of crystals from completely native proteins as well as the screening of different cellular compartments to maximize chances for protein crystallization. By optimizing cloning procedures, recombinant virus production, crystallization and crystal detection, X-ray diffraction data can be collected 24 days after the start of target gene cloning. Furthermore, improved strategies for serial synchrotron diffraction data collection directly from crystals within living cells abolish the need to purify the recombinant protein or the associated microcrystals.

Indexed as

LasersSynchrotronsCrystallizationCrystallography, X-RayRecombinant ProteinsRecombinant Proteins

Identifiers

PMID38402242
PMCPMC10894269

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Registered trials

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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.