Evidence map›Paper›PMID 17098187›Full record

ArticleStructure (London, England : 1993)2006

Lysine methylation as a routine rescue strategy for protein crystallization.

Thomas S Walter, Christoph Meier, Rene Assenberg, Kin-Fai Au, Jingshan Ren, Anil Verma, Joanne E Nettleship, Raymond J Owens, David I Stuart, Jonathan M Grimes

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 163 papers.

0numbers the graph read from it
0cells of the map it votes in
163citing papers in PubMed
9.1field-weighted citation impact, top 1% of its field
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

163 citing papers in PubMed, 271 citations in OpenAlex.

  1. Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
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  5. Crystal structure of the virulence protein J (VirJ) domain 1 from Brucella abortus.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
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  7. Nickel binding to c-Src SH3 domain facilitates crystallization.bioRxiv : the preprint server for biology · 2025
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  10. Comparative studies of seafood and reptile α- and β-parvalbumins.Protein science : a publication of the Protein Society · 2024
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  18. The Impact of Chromate onFrontiers in microbiology · 2022
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  20. Article

103 more citing papers are in PubMed but not listed here.

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

10 authors at 1 institution in 1 country.

Thomas S WalterOxford Protein Production Facility, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, United Kingdom.
Christoph Meier
Rene Assenberg
Kin-Fai Au
Jingshan Ren
Anil Verma
Joanne E Nettleship
Raymond J Owens
David I Stuart
Jonathan M Grimes
Centre for Human Genetics · GB

Funding

Medical Research Council G0400717Wellcome Trust
6 · The paper itself

Abstract

Crystallization remains a critical step in X-ray structure determination. Because it is not generally possible to rationally predict crystallization conditions, commercial screens have been developed which sample a wide range of crystallization space. While this approach has proved successful in many cases, a significant number of proteins fail to crystallize despite being soluble and monodispersed. It is established that chemical modification can facilitate the crystallization of otherwise intractable proteins. Here we describe a method for the reductive methylation of lysine residues which is simple, inexpensive, and efficient, and report on its application to ten proteins. We describe the effect of methylation on the physico-chemical properties of these proteins, and show that it led to diffraction-quality crystals from four proteins and structures for three that had hitherto proved refractory to crystallization. The method is suited to both low- and high-throughput laboratories.

Indexed as

Bacillus anthracisBiochemistryCohort StudiesComputational BiologyCrystallizationCrystallography, X-RayFlavivirusHumansLysineMethylationModels, MolecularMurine hepatitis virusProtein ConformationProteinsLysineProteins

Identifiers

PMID17098187
PMCPMC7126202
OpenAlexW1963829486

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.