Evidence map›Paper›PMID 26841767›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Improving diffraction resolution using a new dehydration method.

Qingqiu Huang, Doletha M E Szebenyi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2016. 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

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

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

2 authors.

Qingqiu HuangMacCHESS, Cornell University, Ithaca, NY 14853, USA.
Doletha M E SzebenyiMacCHESS, Cornell University, Ithaca, NY 14853, USA.

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
NIGMS NIH HHS GM-103485NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

The production of high-quality crystals is one of the major obstacles in determining the three-dimensional structure of macromolecules by X-ray crystallography. It is fairly common that a visually well formed crystal diffracts poorly to a resolution that is too low to be suitable for structure determination. Dehydration has proven to be an effective post-crystallization treatment for improving crystal diffraction quality. Several dehydration methods have been developed, but no single one of them is suitable for all crystals. Here, a new convenient and effective dehydration method is reported that makes use of a dehydrating solution that will not dry out in air for several hours. Using this dehydration method, the resolution of Archaeoglobus fulgidus Cas5a crystals has been increased from 3.2 to 1.95 Å and the resolution of Escherichia coli LptA crystals has been increased from <5 to 3.4 Å.

Indexed as

Archaeal ProteinsArchaeoglobus fulgidusCarrier ProteinsCrystallizationCrystallography, X-RayDehydrationEscherichia coliEscherichia coli ProteinsProtein ConformationArchaeal ProteinsCarrier ProteinsEscherichia coli ProteinsLptA protein, E coliCas5adehydrationdiffraction resolutionLptAprotein crystal

Identifiers

PMID26841767
PMCPMC4741197

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.