Evidence map›Paper›PMID 25573921›Full record

ArticleBioinformatics (Oxford, England)2015

Using isoelectric point to determine the pH for initial protein crystallization trials.

Jobie Kirkwood, David Hargreaves, Simon O'Keefe, Julie Wilson

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Review
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  20. Crystallization of nepenthesin I using a low-pH crystallization screen.Acta crystallographica. Section F, Structural biology communications · 2016
    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

4 authors.

Jobie KirkwoodDepartment of Chemistry, University of York, YO10 5DD, UK, Discovery Sciences, Structure & Biophysics, AstraZeneca Darwin Building, Cambridge, Science Park, Milton Road, Cambridge, CB4 0WG, UK, Department of Computer Science, University of York, YO10 5GH, UK and Department of Mathematics, University of York, YO10 5DD, UK.
David HargreavesDepartment of Chemistry, University of York, YO10 5DD, UK, Discovery Sciences, Structure & Biophysics, AstraZeneca Darwin Building, Cambridge, Science Park, Milton Road, Cambridge, CB4 0WG, UK, Department of Computer Science, University of York, YO10 5GH, UK and Department of Mathematics, University of York, YO10 5DD, UK.
Simon O'KeefeDepartment of Chemistry, University of York, YO10 5DD, UK, Discovery Sciences, Structure & Biophysics, AstraZeneca Darwin Building, Cambridge, Science Park, Milton Road, Cambridge, CB4 0WG, UK, Department of Computer Science, University of York, YO10 5GH, UK and Department of Mathematics, University of York, YO10 5DD, UK.
Julie WilsonDepartment of Chemistry, University of York, YO10 5DD, UK, Discovery Sciences, Structure & Biophysics, AstraZeneca Darwin Building, Cambridge, Science Park, Milton Road, Cambridge, CB4 0WG, UK, Department of Computer Science, University of York, YO10 5GH, UK and Department of Mathematics, University of York, YO10 5DD, UK Department of Chemistry, University of York, YO10 5DD, UK, Discovery Sciences, Structure & Biophysics, AstraZeneca Darwin Building, Cambridge, Science Park, Milton Road, Cambridge, CB4 0WG, UK, Department of Computer Science, University of York, YO10 5GH, UK and Department of Mathematics, University of York, YO10 5DD, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/I015868/1
6 · The paper itself

Abstract

motivationThe identification of suitable conditions for crystallization is a rate-limiting step in protein structure determination. The pH of an experiment is an important parameter and has the potential to be used in data-mining studies to help reduce the number of crystallization trials required. However, the pH is usually recorded as that of the buffer solution, which can be highly inaccurate.

resultsHere, we show that a better estimate of the true pH can be predicted by considering not only the buffer pH but also any other chemicals in the crystallization solution. We use these more accurate pH values to investigate the disputed relationship between the pI of a protein and the pH at which it crystallizes. AVAILABILITY AND IMPLEMENTATION: Data used to generate models are available as Supplementary Material. CONTACT: julie.wilson@york.ac.uk SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

Indexed as

CrystallizationHydrogen-Ion ConcentrationIsoelectric PointProteinsProteins

Identifiers

PMID25573921
PMCPMC4410668

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LicenceCC BY
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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.