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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Abstract
A new software suite, called Crystallography & NMR System (CNS), has been developed for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to existing structure-determination programs, the architecture of CNS is highly flexible, allowing for extension to other structure-determination methods, such as electron microscopy and solid-state NMR spectroscopy. CNS has a hierarchical structure: a high-level hypertext markup language (HTML) user interface, task-oriented user input files, module files, a symbolic structure-determination language (CNS language), and low-level source code. Each layer is accessible to the user. The novice user may just use the HTML interface, while the more advanced user may use any of the other layers. The source code will be distributed, thus source-code modification is possible. The CNS language is sufficiently powerful and flexible that many new algorithms can be easily implemented in the CNS language without changes to the source code. The CNS language allows the user to perform operations on data structures, such as structure factors, electron-density maps, and atomic properties. The power of the CNS language has been demonstrated by the implementation of a comprehensive set of crystallographic procedures for phasing, density modification and refinement. User-friendly task-oriented input files are available for nearly all aspects of macromolecular structure determination by X-ray crystallography and solution NMR.
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(2000) · Nature Structural Biology · doi:10.1038/74028 · Cited by 80
Radom, C. T., Banerjee, A., & Verdine, G. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608989200 · Cited by 75
Dryla, A., Hoffmann, B., Gelbmann, D., Giefing, C., Hanner, M., Meinke, A., Anderson, A. S., Koppensteiner, W., Konrat, R., von Gabain, A., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.01366-06 · Cited by 73
Crystal structure of archaeal RNase HII: a homologue of human major RNase H
Lai, L., Yokota, H., Hung, L.-W., Kim, R., & Kim, S.-H. (2000) · Structure · doi:10.1016/s0969-2126(00)00179-9 · Cited by 71
Jeong, J.-H., Lee, K.-H., Kim, Y.-M., Kim, D.-H., Oh, B.-H., & Kim, Y.-G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c112.384420 · Cited by 68
“ModelbuildingandrefinementwereperformedusingCoot (9) and CNS (10), respectively.”
Structural Basis for Inhibitor-Induced Aggregation of HIV Integrase
Gupta, K., Turkki, V., Sherrill-Mix, S., Hwang, Y., Eilers, G., Taylor, L., McDanal, C., Wang, P., Temelkoff, D., Nolte, R. T., et al. (2016) · PLOS Biology · doi:10.1371/journal.pbio.1002584 · Cited by 68
Premkumar, L., Bobkov, A. A., Patel, M., Jaroszewski, L., Bankston, L. A., Stec, B., Vuori, K., Côté, J.-F., & Liddington, R. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102517 · Cited by 68
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
Structural Basis for Phosphotyrosine Recognition by Suppressor of Cytokine Signaling-3
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Lamb, D. C., Kim, Y., Yermalitskaya, L. V., Yermalitsky, V. N., Lepesheva, G. I., Kelly, S. L., Waterman, M. R., & Podust, L. M. (2006) · Structure · doi:10.1016/j.str.2005.09.015 · Cited by 60
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Metadata
- Authors
- 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., Read, R. J., Rice, L. M., Simonson, T., & Warren, G. L.
- Venue
- Acta Crystallographica Section D Biological Crystallography
- Published
- 1998-09-01
- Volume
- 54
- Issue
- 5
- Pages
- 905-921
- ISSN
- 0907-4449 (ISSN-L)
- OpenAlex
- W1995017064
- Cited by
- 15,715
- References
- 0
- FWCI
- 489.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- journals.iucr.org/services/copyrightpolicy.html (vor)
- journals.iucr.org/services/copyrightpolicy.html#TDM (tdm)
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.
