Evidence map›Paper›PMID 41842660›Full record

ArticleActa crystallographica. Section F, Structural biology communications2026

Optimized bacterial expression of a synthetic BRIL antibody.

Benjamin F Cooper, Georgia L Isom

Abstract read
In one paragraph

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

2 authors.

Benjamin F CooperSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Georgia L IsomSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.

Funding

European Research Council, H2020 European Research Council 101162143Medical Research Council MR/W016672/1
6 · The paper itself

Abstract

The use of monoclonal fragments antigen binding (Fabs) is a prevalent methodology facilitating protein structure determination via both crystallography and cryo-EM. The development of a synthetic Fab against the BRIL domain improved the accessibility of this approach, providing a general fiducial applicable to any protein of interest via the simple curation of a BRIL fusion protein. Here, we document the generation of a T7 Express ΔcybC strain allowing contaminant-free bacterial expression of the synthetic anti-BRIL Fab BAG2. We also report the crystal structure of BAG2 in complex with native cytochrome b

Indexed as

Escherichia coliImmunoglobulin Fab FragmentsCryoelectron MicroscopyCrystallography, X-RayGene ExpressionModels, MolecularRecombinant Fusion ProteinsImmunoglobulin Fab FragmentsRecombinant Fusion ProteinsBRILcryo-EMfiducialssynthetic antibodiesX-ray crystallography

Identifiers

PMID41842660
PMCPMC13041623

What OpenQuestion holds

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LicenceCC BY
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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.