The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Specific chemical and structural damage to proteins produced by synchrotron radiation
Open accessAbstract
Radiation damage is an inherent problem in x-ray crystallography. It usually is presumed to be nonspecific and manifested as a gradual decay in the overall quality of data obtained for a given crystal as data collection proceeds. Based on third-generation synchrotron x-ray data, collected at cryogenic temperatures, we show for the enzymes Torpedo californica acetylcholinesterase and hen egg white lysozyme that synchrotron radiation also can cause highly specific damage. Disulfide bridges break, and carboxyl groups of acidic residues lose their definition. Highly exposed carboxyls, and those in the active site of both enzymes, appear particularly susceptible. The catalytic triad residue, His-440, in acetylcholinesterase, also appears to be much more sensitive to radiation damage than other histidine residues. Our findings have direct practical implications for routine x-ray data collection at high-energy synchrotron sources. Furthermore, they provide a direct approach for studying the radiation chemistry of proteins and nucleic acids at a detailed, structural level and also may yield information concerning putative “weak links” in a given biological macromolecule, which may be of structural and functional significance.
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.
Integrity signals
Registry
Cites
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.
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
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
Self-citationMOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085
Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,648
Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., & Silman, I. (1991) · Science · doi:10.1126/science.1678899 · Cited by 2,707
Self-citationRaster3D Version 2.0. A program for photorealistic molecular graphics
Merritt, E. A., & Murphy, M. E. P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994006396 · Cited by 2,504
Improved Fourier coefficients for maps using phases from partial structures with errors
Read, R. J. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099622 · Cited by 1,873
The chemical basis of radiation biology
von Sonntag, C. (1987) · Medical Entomology and Zoology · Cited by 1,760
Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron Radiation
Hendrickson, W. A. (1991) · Science · doi:10.1126/science.1925561 · Cited by 1,129
Esnouf, R. M. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998017363 · Cited by 753
Sussman, J. L., Lin, D., Jiang, J., Manning, N. O., Prilusky, J., Ritter, O., & Abola, E. E. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998009378 · Cited by 740
Self-citation
Cited by
Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
Kunishima, N., Shimada, Y., Tsuji, Y., Sato, T., Yamamoto, M., Kumasaka, T., Nakanishi, S., Jingami, H., & Morikawa, K. (2000) · Nature · doi:10.1038/35039564 · Cited by 1,249
Structural definition of a conserved neutralization epitope on HIV-1 gp120
Zhou, T., Xu, L., Dey, B., Hessell, A. J., Van Ryk, D., Xiang, S.-H., Yang, X., Zhang, M.-Y., Zwick, M. B., Arthos, J., et al. (2007) · Nature · doi:10.1038/nature05580 · Cited by 770
Smart, O. S., Womack, T. O., Flensburg, C., Keller, P., Paciorek, W., Sharff, A., Vonrhein, C., & Bricogne, G. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911056058 · Cited by 612
Polymerization Reactions and Modifications of Polymers by Ionizing Radiation
Ashfaq, A., Clochard, M.-C., Coqueret, X., Dispenza, C., Driscoll, M. S., Ulański, P., & Al-Sheikhly, M. (2020) · Polymers · doi:10.3390/polym12122877 · Cited by 459
Quantitative Speciation of Heavy Metals in Soils and Sediments by Synchrotron X-ray Techniques
Manceau, A., Marcus, M. A., & Tamura, N. (2002) · Reviews in Mineralogy and Geochemistry · doi:10.2138/gsrmg.49.1.341 · Cited by 451
Metadata
- Authors
- Weik, M., Ravelli, R. B. G., Kryger, G., McSweeney, S., Raves, M. L., Harel, M., Gros, P., Silman, I., Kroon, J., & Sussman, J. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-01-18
- Volume
- 97
- Issue
- 2
- Pages
- 623-628
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2127432350
- Cited by
- 444
- References
- 27
- FWCI
- 12.46
- Type
- journal article
- Language
- en
- Open access
- green
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Specific chemical and structural damage to proteins produced by synchrotron radiation. https://app.cochat.ai/papers/10.1073/pnas.97.2.623
- The paper
- Weik, M., Ravelli, R. B. G., Kryger, G., McSweeney, S., Raves, M. L., Harel, M., Gros, P., Silman, I., Kroon, J., & Sussman, J. L. (2000). Specific chemical and structural damage to proteins produced by synchrotron radiation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.2.623
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.