Evidence map›Paper›PMID 23027760›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012

Purification, crystallization and preliminary crystallographic analysis of Kar9p from Saccharomyces cerevisiae.

Daniela Hüls, Dierk Niessing

Abstract 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. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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.

Daniela HülsInstitute of Structural Biology, Helmholtz Zentrum München, German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
Dierk Niessing

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kar9p is required for correct positioning of the mitotic spindle in Saccharomyces cerevisiae. The in vivo function of Kar9p is well understood, but no structural information is available. Additionally, molecular details of how Kar9p interacts with other proteins are scarce. Full-length Kar9p was expressed in Escherichia coli, purified and crystallized. Diffraction data were collected and processed at 7 Å resolution. One crystal showed diffraction to 3 Å resolution. The crystals that diffracted to 7 Å resolution belonged to space group P3, with unit-cell parameters a = b = 195.02, c = 257.15 Å, α = β = 90, γ = 120°. The crystal that diffracted to 3 Å resolution belonged to space group P222, with unit-cell parameters a = 46.37, b = 74.64, c = 133.63 Å, α = β = γ = 90°.

Indexed as

CrystallizationCrystallography, X-RayNuclear ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsKAR9 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID23027760
PMCPMC3497990

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.