The DOI matches its Crossref record.
Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron Radiation
Abstract
Resonance between beams of x-ray waves and electronic transitions from bound atomic orbitals leads to a phenomenon known as anomalous scattering. This effect can be exploited in x-ray crystallographic studies on biological macromolecules by making diffraction measurements at selected wavelengths associated with a particular resonant transition. In this manner the problem of determining the three-dimensional structure of thousands of atoms is reduced to that of initially solving for a few anomalous scattering centers that can then be used as a reference for developing the entire structure. This method of multiwavelength anomalous diffraction has now been applied in a number of structure determinations. Optimal experiments require appropriate synchrotron instrumentation, careful experimental design, and sophisticated analytical procedures. There are rich opportunities for future applications.
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
Cited by
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417
Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891
Siderophore-Mediated Iron Transport: Crystal Structure of FhuA with Bound Lipopolysaccharide
Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., & Welte, W. (1998) · Science · doi:10.1126/science.282.5397.2215 · Cited by 787
Transmembrane Signaling across the Ligand-Gated FhuA Receptor
Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P., & Moras, D. (1998) · Cell · doi:10.1016/s0092-8674(00)81700-6 · Cited by 540
Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA
Chen, L., Glover, J. N. M., Hogan, P. G., Rao, A., & Harrison, S. C. (1998) · Nature · doi:10.1038/32100 · Cited by 521
Structure of IRF-1 with bound DNA reveals determinants of interferon regulation
Escalante, C. R., Yie, J., Thanos, D., & Aggarwal, A. K. (1998) · Nature · doi:10.1038/34224 · Cited by 397
Structural basis of gating by the outer membrane transporter FecA
Ferguson, A. D., Chakraborty, R., Smith, B. S., Esser, L., van der Helm, D., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1067313 · Cited by 373
Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions
Crane, B. R., Siegel, L. M., & Getzoff, E. D. (1995) · Science · doi:10.1126/science.270.5233.59 · Cited by 345
Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
Worthylake, D. K., Wang, H., Yoo, S., Sundquist, W. I., & Hill, C. P. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998007689 · Cited by 235
Dann, C. E., Bruick, R. K., & Deisenhofer, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202614999 · Cited by 200
Haem recognition by a Staphylococcus aureus NEAT domain
Grigg, J. C., Vermeiren, C. L., Heinrichs, D. E., & Murphy, M. E. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05502.x · Cited by 166
Romanowski, M. J., Soccio, R. E., Breslow, J. L., & Burley, S. K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052140699 · Cited by 162
Hyman, J., Chen, H., Di Fiore, P. P., De Camilli, P., & Brunger, A. T. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.537 · Cited by 158
Crystal structure of PU. 1/IRF-4/DNA ternary complex
Escalante, C. R., Brass, A. L., Pongubala, J. M. R., Shatova, E., Shen, L., Singh, H., & Aggarwal, A. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00703-7 · Cited by 154
Zhang, Z., Lee, C., Mandiyan, V., Borg, J., Margolis, B., Schlessinger, J., & Kuriyan, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.20.6141 · Cited by 140
Multiwavelength Anomalous Diffraction at High X-Ray Intensity
Son, S.-K., Chapman, H. N., & Santra, R. (2011) · Physical Review Letters · doi:10.1103/physrevlett.107.218102 · Cited by 120
Ceccarelli, C., Grodsky, N. B., Ariyaratne, N., Colman, R. F., & Bahnson, B. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207306200 · Cited by 116
Molecular basis for sterol transport by StART‐like lipid transfer domains
Horenkamp, F. A., Valverde, D. P., Nunnari, J., & Reinisch, K. M. (2018) · The EMBO Journal · doi:10.15252/embj.201798002 · Cited by 113
Gong, R., Li, L., Liu, Y., Wang, P., Yang, H., Wang, L., Cheng, J., Guan, K.-L., & Xu, Y. (2011) · Genes & Development · doi:10.1101/gad.16968011 · Cited by 98
Recognition of protein-linked glycans as a determinant of peptidase activity
Noach, I., Ficko-Blean, E., Pluvinage, B., Stuart, C., Jenkins, M. L., Brochu, D., Buenbrazo, N., Wakarchuk, W., Burke, J. E., Gilbert, M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615141114 · Cited by 89
Underwood, K. W., Parris, K. D., Federico, E., Mosyak, L., Czerwinski, R. M., Shane, T., Taylor, M., Svenson, K., Liu, Y., Hsiao, C.-L., et al. (2003) · Structure · doi:10.1016/s0969-2126(03)00092-3 · Cited by 62
Integrative Structural Biology in the Era of Accurate Structure Prediction
Masrati, G., Landau, M., Ben-Tal, N., Lupas, A., Kosloff, M., & Kosinski, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167127 · Cited by 53
Computational models in the service of X‐ray and cryo‐ electron microscopy structure determination
Kryshtafovych, A., Moult, J., Albrecht, R., Chang, G. A., Chao, K., Fraser, A., Greenfield, J., Hartmann, M. D., Herzberg, O., Josts, I., et al. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26223 · Cited by 45
Gualtieri, A. F., Andreozzi, G. B., Tomatis, M., & Turci, F. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.023 · Cited by 45
Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5
Tao, X., & Tong, L. (2007) · Protein Science · doi:10.1110/ps.062712807 · Cited by 31
Malmirchegini, G. R., Sjodt, M., Shnitkind, S., Sawaya, M. R., Rosinski, J., Newton, S. M., Klebba, P. E., & Clubb, R. T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.583013 · Cited by 33
Metadata
- Authors
- Hendrickson, W. A.
- Venue
- Science
- Published
- 1991-10-04
- Volume
- 254
- Issue
- 5028
- Pages
- 51-58
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1969156185
- Cited by
- 1,129
- References
- 0
- FWCI
- 11.65
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.