Evidence map›Paper›PMID 40517138›Full record

ArticleNPJ microgravity2025

Exploring the potential of a bioassembler for protein crystallization in space.

Christopher MacCarthy, Elizaveta Koudan, Mikhail Shevtsov, Vladislav Parfenov, Stanislav Petrov, Aleksandr Levin, Fedor Senatov, Nina Sykilinda, Sergey Ostrovskiy, Stanislav Pekov and 9 more

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PubMed Full text at PMC Publisher
In one paragraph

Article in NPJ microgravity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
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

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

1 citing paper in PubMed.

  1. 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

19 authors.

Christopher MacCarthy *Moscow Institute of Physics and Technology, Dolgoprudny, Russia.ORCID http://orcid.org/0000-0001-9766-9808
Elizaveta Koudan *National University of Science and Technology MISIS, Moscow, Russia.ORCID http://orcid.org/0000-0001-9377-8118
Mikhail ShevtsovMoscow Institute of Physics and Technology, Dolgoprudny, Russia.
Vladislav ParfenovLaboratory for Biotechnological Research "3D Bioprinting Solutions", Moscow, Russia.
Stanislav PetrovNational University of Science and Technology MISIS, Moscow, Russia.
Aleksandr LevinNational University of Science and Technology MISIS, Moscow, Russia.
Fedor SenatovNational University of Science and Technology MISIS, Moscow, Russia.
Nina SykilindaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia.
Sergey OstrovskiyNational University of Science and Technology MISIS, Moscow, Russia.
Stanislav PekovSkolkovo Institute of Science and Technology, Moscow, Russia.
Ivan GushchinMoscow Institute of Physics and Technology, Dolgoprudny, Russia.
Igor PopovMoscow Institute of Physics and Technology, Dolgoprudny, Russia.
Egor ZinovevMoscow Institute of Physics and Technology, Dolgoprudny, Russia.
Andrey BogorodskiyMoscow Institute of Physics and Technology, Dolgoprudny, Russia.
Alexey MishinMoscow Institute of Physics and Technology, Dolgoprudny, Russia.
Valentin IvanovichMoscow Institute of Physics and Technology, Dolgoprudny, Russia.
Andrey RogachevMoscow Institute of Physics and Technology, Dolgoprudny, Russia.
Yusef KhesuaniLaboratory for Biotechnological Research "3D Bioprinting Solutions", Moscow, Russia. usefhesuani@yandex.ru.
Valentin BorshchevskiyMoscow Institute of Physics and Technology, Dolgoprudny, Russia. borshchevskiy.vi@phystech.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein crystallization holds paramount significance in structural biology, serving as a pivotal technique for unveiling the three-dimensional (3D) architecture of proteins. While microgravity conditions in space offer distinct advantages for high-quality protein crystal growth by mitigating the influences of gravity and convection, the development of reliable techniques for protein crystallization in space with precise control over the crystallization process and its meticulous inspections remains a challenge. In this study, we present an innovative bioassembler-specifically, the 'Organ.Aut'-which we successfully employed to crystallize protein in space. The bioassembler 'Organ.Aut' produced highly ordered crystals diffracted to a true-atomic resolution of ∼1 Å. These data allowed for a detailed examination of atomic structures, enabling thorough structural comparisons with crystals grown on Earth. Our finding suggests that the bioassembler 'Organ.Aut' stands as a promising and viable option for advancing protein crystallization in space.

Identifiers

PMID40517138
PMCPMC12167385

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