Evidence map›Paper›PMID 19574640›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009

Crystallization and preliminary X-ray diffraction studies of the tetramerization domain derived from the human potassium channel Kv1.3.

Andreas Winklmeier, Michael Weyand, Christina Schreier, Hans Robert Kalbitzer, Werner Kremer

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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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

1 citing paper in PubMed.

  1. 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

5 authors.

Andreas WinklmeierDepartment of Biophysics and Physical Biochemistry, University of Regensburg, D-93040 Regensburg, Germany.
Michael Weyand
Christina Schreier
Hans Robert Kalbitzer
Werner Kremer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tetramerization domain (T1 domain) derived from the voltage-dependent potassium channel Kv1.3 of Homo sapiens was recombinantly expressed in Escherichia coli and purified. The crystals were first grown in an NMR tube in 150 mM potassium phosphate pH 6.5 in the absence of additional precipitants. The crystals showed I4 symmetry characteristic of the naturally occurring tetrameric assembly of the single subunits. A complete native data set was collected to 1.2 A resolution at 100 K using synchrotron radiation.

Indexed as

Protein MultimerizationX-Ray DiffractionCrystallizationHumansKv1.3 Potassium ChannelProtein Structure, TertiaryKv1.3 Potassium Channel

Identifiers

PMID19574640
PMCPMC2705635

What OpenQuestion holds

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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.