Evidence map›Paper›PMID 24419635›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Measurement of the intrinsic variability within protein crystals: implications for sample-evaluation and data-collection strategies.

Michael G Bowler, Matthew W Bowler

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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  5. Article
  6. Fully automatic characterization and data collection from crystals of biological macromolecules.Acta crystallographica. Section D, Biological crystallography · 2015
    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.

Michael G BowlerDepartment of Physics, University of Oxford, Keble Road, Oxford OX1 3RH, England.
Matthew W BowlerEuropean Molecular Biology Laboratory, Grenoble Outstation, 6 Rue Jules Horowitz, 38042 Grenoble, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The advent of micro-focused X-ray beams has led to the development of a number of advanced methods of sample evaluation and data collection. In particular, multiple-position data-collection and helical oscillation strategies are now becoming commonplace in order to alleviate the problems associated with radiation damage. However, intra-crystal and inter-crystal variation means that it is not always obvious on which crystals or on which region or regions of a crystal these protocols should be performed. For the automation of this process for large-scale screening, and to provide an indication of the best strategy for data collection, a metric of crystal variability could be useful. Here, measures of the intrinsic variability within protein crystals are presented and their implications for optimal data-collection strategies are discussed.

Indexed as

AnimalsCattleCrystallizationCrystallography, X-RayHumansProteinsProton-Translocating ATPasesrhoA GTP-Binding ProteinProteinsProton-Translocating ATPasesrhoA GTP-Binding Proteinautomationmacromolecular crystallographymicrofocussample evaluation

Identifiers

PMID24419635
PMCPMC3943112

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.