Evidence map›Paper›PMID 41324409›Full record

ArticleActa crystallographica. Section F, Structural biology communications2026

Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein.

Christina Geerds, Hartmut H Niemann

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.

Christina GeerdsDepartment of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.
Hartmut H NiemannDepartment of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.ORCID 0000-0002-8582-0360

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This case report describes single surface substitutions that improve the crystallizability and diffraction properties of a flexible two-domain protein. InlB

Indexed as

CrystallizationGlutamic AcidTyrosineAmino Acid SequenceBacterial ProteinsCrystallography, X-RayListeria monocytogenesModels, MolecularProtein DomainsBacterial ProteinsGlutamic AcidTyrosinecrystal contactsmultidomain proteinspoint mutationsprotein crystallizationsurface-entropy reductionsurface mutation

Identifiers

PMID41324409
PMCPMC12809440

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.