Evidence map›Paper›PMID 40227217›Full record

ArticleActa crystallographica. Section F, Structural biology communications2025

Crystallization and initial X-ray crystallographic analysis of a de novo-designed protein with left-handed βαβ units.

Naoki Tomita, Riu Hirano, Hiroto Murata, Yasufumi Umena, Hiroki Onoda, George Chikenji, Leonard M G H Chavas

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2025. 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

7 authors.

Naoki TomitaDepartment of Applied Physics, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.
Riu HiranoDepartment of Applied Physics, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.
Hiroto MurataDepartment of Applied Physics, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.ORCID 0000-0002-8931-5898
Yasufumi UmenaSynchrotron Radiation Research Center, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.
Hiroki OnodaSynchrotron Radiation Research Center, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.
George ChikenjiDepartment of Applied Physics, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.
Leonard M G H ChavasDepartment of Applied Physics, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.ORCID 0000-0001-9973-9355

Funding

Japan Agency for Medical Research and Development JP23ama121001
6 · The paper itself

Abstract

A newly designed protein featuring a rare left-handed βαβ motif has successfully been crystallized and characterized by preliminary X-ray diffraction. The computational design was conducted using a combination of Rosetta BluePrintBDR, ProteinMPNN and AlphaFold2, generating eight candidates based on predicted stability and folding accuracy. The final construct was expressed, purified and crystallized in space group P2

Indexed as

ProteinsAmino Acid SequenceCrystallizationCrystallography, X-RayEscherichia coliModels, MolecularProtein Conformation, beta-StrandProteinsAlphaFoldde novo protein designleft-handed βαβ motifX-ray crystallography

Identifiers

PMID40227217
PMCPMC12035557

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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.