Evidence map›Paper›PMID 22505411›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012

Purification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria monocytogenes.

Kim Langmach Hein, Poul Nissen, Jens Preben Morth

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Mimer: an automated spreadsheet-based crystallization screening system.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    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

3 authors at 3 institutions in 2 countries.

Kim Langmach HeinCentre for Molecular Medicine Norway, University of Oslo, PO Box 1137 Blindern, 0318 Oslo, Norway. kimlan@ncmm.uio.no
Poul Nissen
Jens Preben Morth
Aarhus University · DKOslo University Hospital · NOUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ca(2+)-ATPases are members of a large family of membrane proteins that maintain the selective movement of cations across biological membranes. A putative Listeria monocytogenes Ca(2+)-ATPase (Lmo0818) was crystallized in an unknown functional state. The crystal belonged to space group P2(1)2(1)2(1) and a complete data set was collected to 3.2 Å resolution. The molecular-replacement solution obtained revealed that Lmo0818 is likely to adopt an E2-like state mimicking the phosphorylated intermediate in the functional cycle of the sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) and a stacked bilayer `type I' packing in the crystal.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceCrystallizationCrystallography, X-RayListeria monocytogenesModels, MolecularProtein Structure, QuaternarySequence AlignmentAdenosine Triphosphatases

Identifiers

PMID22505411
PMCPMC3325811
OpenAlexW2076975927

What OpenQuestion holds

Textmetadata
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.