Evidence map›Paper›PMID 33263568›Full record

ArticleActa crystallographica. Section F, Structural biology communications2020

The A component (SmhA) of a tripartite pore-forming toxin from Serratia marcescens: expression, purification and crystallographic analysis.

Alicia M Churchill-Angus, Svetlana E Sedelnikova, Thomas H B Schofield, Patrick J Baker

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.0field-weighted citation impact, top 58% of its field
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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. 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

4 authors at 2 institutions in 1 country.

Alicia M Churchill-AngusDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Western Bank, Sheffield S10 2TN, United Kingdom.ORCID 0000-0003-0918-2333
Svetlana E SedelnikovaDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Western Bank, Sheffield S10 2TN, United Kingdom.
Thomas H B SchofieldDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Western Bank, Sheffield S10 2TN, United Kingdom.ORCID 0000-0002-3795-0574
Patrick J BakerDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Western Bank, Sheffield S10 2TN, United Kingdom.ORCID 0000-0003-1995-5643
University of Sheffield · GBUniversity of Leeds · GB

Funding

Engineering and Physical Sciences Research Council EP/L026872/1
6 · The paper itself

Abstract

Tripartite α-pore-forming toxins are constructed of three proteins (A, B and C) and are found in many bacterial pathogens. While structures of the B and C components from Gram-negative bacteria have been described, the structure of the A component of a Gram-negative α-pore-forming toxin has so far proved elusive. SmhA, the A component from the opportunistic human pathogen Serratia marcescens, has been cloned, overexpressed and purified. Crystals were grown of selenomethionine-derivatized protein and anomalous data were collected. Phases were calculated and an initial electron-density map was produced.

Indexed as

Bacterial ToxinsCloning, MolecularCrystallography, X-RaySerratia marcescensBacterial ToxinsClyA familycrystallizationpore-forming toxinSerratia

Identifiers

PMID33263568
PMCPMC7716259
OpenAlexW3110329461

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.