Evidence map›Paper›PMID 26960118›Full record

ReviewActa crystallographica. Section D, Structural biology2016

An overview of heavy-atom derivatization of protein crystals.

Ashley C W Pike, Elspeth F Garman, Tobias Krojer, Frank von Delft, Elisabeth P Carpenter

Abstract readReview
In one paragraph

Review in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

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  17. High-throughput in situ experimental phasing.Acta crystallographica. Section D, Structural biology · 2020
    Article
  18. Article
  19. X-ray and UV radiation-damage-induced phasing using synchrotron serial crystallography.Acta crystallographica. Section D, Structural biology · 2018
    Article
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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

5 authors.

Ashley C W PikeStructural Genomics Consortium, University of Oxford, Roosevelt Drive, Oxford OX11 9HP, England.
Elspeth F GarmanDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England.
Tobias KrojerStructural Genomics Consortium, University of Oxford, Roosevelt Drive, Oxford OX11 9HP, England.
Frank von DelftStructural Genomics Consortium, University of Oxford, Roosevelt Drive, Oxford OX11 9HP, England.
Elisabeth P CarpenterStructural Genomics Consortium, University of Oxford, Roosevelt Drive, Oxford OX11 9HP, England.

Funding

CIHRMedical Research Council MR/L017458/1Wellcome TrustWellcome Trust 092809/Z/10/Z
6 · The paper itself

Abstract

Heavy-atom derivatization is one of the oldest techniques for obtaining phase information for protein crystals and, although it is no longer the first choice, it remains a useful technique for obtaining phases for unknown structures and for low-resolution data sets. It is also valuable for confirming the chain trace in low-resolution electron-density maps. This overview provides a summary of the technique and is aimed at first-time users of the method. It includes guidelines on when to use it, which heavy atoms are most likely to work, how to prepare heavy-atom solutions, how to derivatize crystals and how to determine whether a crystal is in fact a derivative.

Indexed as

AnimalsBromineCrystallography, X-RayHumansIodineMetals, HeavyMethionineNoble GasesProtein ConformationProteinsSelenomethionineBromineIodineMetals, HeavyMethionineNoble GasesProteinsSelenomethioninecrystallographyderivatization of crystalsheavy atomsphasing techniquesprotein crystals

Identifiers

PMID26960118
PMCPMC4784662

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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.