Evidence map›Paper›PMID 37158197›Full record

ArticleActa crystallographica. Section D, Structural biology2023

GEMMI and Servalcat restrain REFMAC5.

Keitaro Yamashita, Marcin Wojdyr, Fei Long, Robert A Nicholls, Garib N Murshudov

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Porcine serum maltase-glucoamylase: structure, kinetics, and inhibition.Journal of enzyme inhibition and medicinal chemistry · 2026
    Article
  2. Article
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Multicyclic D-Stereospecific Hydrolase Dimer With High Sustained Activity.Angewandte Chemie (International ed. in English) · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Crystal structure of a tRNA acceptor-stem mimic at 1.94 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Doublet decoding of tRNANature communications · 2025
    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

5 authors.

Keitaro YamashitaMRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Trumpington, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0002-5442-7582
Marcin WojdyrGlobal Phasing Ltd, Cambridge, United Kingdom.ORCID 0000-0003-3980-4092
Fei LongMRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Trumpington, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0002-2553-9841
Robert A NichollsMRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Trumpington, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0002-8577-8617
Garib N MurshudovMRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Trumpington, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0001-6483-3587

Funding

Biotechnology and Biological Sciences Research Council BB/S007083/1Medical Research Council MC_UP_A025_1012
6 · The paper itself

Abstract

Macromolecular refinement uses experimental data together with prior chemical knowledge (usually digested into geometrical restraints) to optimally fit an atomic structural model into experimental data, while ensuring that the model is chemically plausible. In the CCP4 suite this chemical knowledge is stored in a Monomer Library, which comprises a set of restraint dictionaries. To use restraints in refinement, the model is analysed and template restraints from the dictionary are used to infer (i) restraints between concrete atoms and (ii) the positions of riding hydrogen atoms. Recently, this mundane process has been overhauled. This was also an opportunity to enhance the Monomer Library with new features, resulting in a small improvement in REFMAC5 refinement. Importantly, the overhaul of this part of CCP4 has increased flexibility and eased experimentation, opening up new possibilities.

Indexed as

ProteinsSoftwareCrystallography, X-RayMacromolecular SubstancesModels, MolecularProtein ConformationMacromolecular SubstancesProteinsGEMMImodel refinementREFMAC5Servalcat

Identifiers

PMID37158197
PMCPMC10167671

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.