Cited by 5Enzyme Structure and FunctionProtein Structure and DynamicsAdvanced Electron Microscopy Techniques and Applications

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Sequence-assignment validation in protein crystal structure models with checkMySequence

Open access
Chojnowski, Grzegorz·2023·Acta Crystallographica Section D Structural Biology

Published version of a preprint

Abstract

Sequence-register shifts remain one of the most elusive errors in experimental macromolecular models. They may affect model interpretation and propagate to newly built models from older structures. In a recent publication, it was shown that register shifts in cryo-EM models of proteins can be detected using a systematic reassignment of short model fragments to the target sequence. Here, it is shown that the same approach can be used to detect register shifts in crystal structure models using standard, model-bias-corrected electron-density maps (2 mF o − DF c ). Five register-shift errors in models deposited in the PDB detected using this method are described in detail.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1107/s2059798323003765

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 36

  1. Armstrong, 2020, Nucleic Acids Res., 48, D335
  2. Baek, 2021, Science, 373, 871, 10.1126/science.abj8754 · DOI · Paper page
  3. Brünger, 1992, Nature, 355, 472, 10.1038/355472a0 · DOI
  4. Brzezinski, 2020, FEBS J., 287, 2685, 10.1111/febs.15314 · DOI
  5. Burley, 2019, Nucleic Acids Res., 47, D464, 10.1093/nar/gky1004 · DOI
  6. Casañal, 2020, Protein Sci., 29, 1055, 10.1002/pro.3791 · DOI
  7. Caserta, 2017, Nat. Chem. Biol., 13, 779, 10.1038/nchembio.2385 · DOI
  8. Chojnowski, 2022, Acta Cryst. D, 78, 806, 10.1107/S2059798322005009 · DOI · Paper page
  9. Chojnowski, 2022, IUCrJ, 9, 86, 10.1107/S2052252521011088 · DOI
  10. Croll, 2021, Biophys. J., 120, 1085, 10.1016/j.bpj.2020.12.029 · DOI
  11. DeLano, 2002, CCP4 Newsl. Protein Crystallogr., 40, 82
  12. Gore, 2017, Structure, 25, 1916, 10.1016/j.str.2017.10.009 · DOI
  13. Hooft, 1996, Nature, 381, 272, 10.1038/381272a0 · DOI
  14. Hunter, 2007, Comput. Sci. Eng., 9, 90, 10.1109/MCSE.2007.55 · DOI · Paper page
  15. Jones, 2022, Nat. Methods, 19, 15, 10.1038/s41592-021-01365-3 · DOI
  16. Joosten, 2014, IUCrJ, 1, 213, 10.1107/S2052252514009324 · DOI
  17. Kashav, 2009, PLoS One, 4, e7515, 10.1371/journal.pone.0007515 · DOI
  18. Kissinger, 2001, Acta Cryst. D, 57, 1474, 10.1107/S0907444901012458 · DOI
  19. Krissinel, 2012, J. Mol. Biochem., 1, 76
  20. Krissinel, 2022, Acta Cryst. D, 78, 1079, 10.1107/S2059798322007987 · DOI
  21. Laskowski, 1993, J. Appl. Cryst., 26, 283, 10.1107/S0021889892009944 · DOI · Paper page
  22. McCoy, 2007, J. Appl. Cryst., 40, 658, 10.1107/S0021889807021206 · DOI · Paper page
  23. Murshudov, 2011, Acta Cryst. D, 67, 355, 10.1107/S0907444911001314 · DOI
  24. Paysan-Lafosse, 2022, Nucleic Acids Res., 51, D418, 10.1093/nar/gkac993 · DOI
  25. Prisant, 2020, Protein Sci., 29, 315, 10.1002/pro.3786 · DOI
  26. Read, 1986, Acta Cryst. A, 42, 140, 10.1107/S0108767386099622 · DOI
  27. Sánchez Rodríguez, 2022, Acta Cryst. D, 78, 1412, 10.1107/S2059798322010415 · DOI · Paper page
  28. Shen, 2018, Sci. Rep., 8, 12965, 10.1038/s41598-018-31140-y · DOI
  29. Sobolev, 2020, Structure, 28, 1249, 10.1016/j.str.2020.08.005 · DOI
  30. Tickle, 1998, Acta Cryst. D, 54, 243, 10.1107/S090744499701041X · DOI
  31. Tu, 2005, Cell, 121, 257, 10.1016/j.cell.2005.02.005 · DOI
  32. Varadi, 2022, Nucleic Acids Res., 50, D439, 10.1093/nar/gkab1061 · DOI · Paper page
  33. Williams, 2018, Protein Sci., 27, 293, 10.1002/pro.3330 · DOI · Paper page
  34. Wlodawer, 2018, FEBS J., 285, 444, 10.1111/febs.14320 · DOI
  35. wwPDB Consortium, 2018, Nucleic Acids Res., 47, D520, 10.1093/nar/gky949 · DOI · Paper page
  36. Yang, 2016, J. Appl. Cryst., 49, 1081, 10.1107/S1600576716004428 · DOI

Metadata

Authors
Chojnowski, G.
Affiliations
European Molecular Biology Laboratory (DE)
Corresponding author
Chojnowski, Grzegorz
Venue
Acta Crystallographica Section D Structural Biology
Published
2023-06-14
Volume
79
Issue
7
Pages
559-568
ISSN
2059-7983 (ISSN-L)
OpenAlex
W4380575664
Cited by
5
References
3
Citations by year
2025: 3 · 2024: 2
FWCI
0.37
Type
journal article
Language
en
Open access
Locations
  • Acta Crystallographica Section D Structural Biology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Keywords
model validation, electron density maps, model bias correction
MeSH terms
Models, Molecular, Protein Conformation, Proteins, Cryoelectron Microscopy, Macromolecular Substances

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review