Evidence map›Paper›PMID 26413539›Full record

ReviewBioMed research international2015

Two-Dimensional Crystallization Procedure, from Protein Expression to Sample Preparation.

Qie Kuang, Pasi Purhonen, Hans Hebert

Abstract readReview
In one paragraph

Review in BioMed research international, 2015. 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

3 authors.

Qie KuangDepartment of Biosciences and Nutrition, Karolinska Institutet, Novum, 14183 Huddinge, Sweden ; School of Technology and Health, KTH Royal Institute of Technology, Novum, 14183 Huddinge, Sweden.
Pasi PurhonenDepartment of Biosciences and Nutrition, Karolinska Institutet, Novum, 14183 Huddinge, Sweden.
Hans HebertDepartment of Biosciences and Nutrition, Karolinska Institutet, Novum, 14183 Huddinge, Sweden ; School of Technology and Health, KTH Royal Institute of Technology, Novum, 14183 Huddinge, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane proteins play important roles for living cells. Structural studies of membrane proteins provide deeper understanding of their mechanisms and further aid in drug design. As compared to other methods, electron microscopy is uniquely suitable for analysis of a broad range of specimens, from small proteins to large complexes. Of various electron microscopic methods, electron crystallography is particularly well-suited to study membrane proteins which are reconstituted into two-dimensional crystals in lipid environments. In this review, we discuss the steps and parameters for obtaining large and well-ordered two-dimensional crystals. A general description of the principle in each step is provided since this information can also be applied to other biochemical and biophysical methods. The examples are taken from our own studies and published results with related proteins. Our purpose is to give readers a more general idea of electron crystallography and to share our experiences in obtaining suitable crystals for data collection.

Indexed as

CrystallizationMembrane ProteinsMicroscopy, ElectronRecombinant ProteinsMembrane ProteinsRecombinant Proteins

Identifiers

PMID26413539
PMCPMC4564634

What OpenQuestion holds

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Registered trials

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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.