The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline
Open accessAbstract
Structural genomics is emerging as a principal approach to define protein structure–function relationships. To apply this approach on a genomic scale, novel methods and technologies must be developed to determine large numbers of structures. We describe the design and implementation of a high-throughput structural genomics pipeline and its application to the proteome of the thermophilic bacterium Thermotoga maritima . By using this pipeline, we successfully cloned and attempted expression of 1,376 of the predicted 1,877 genes (73%) and have identified crystallization conditions for 432 proteins, comprising 23% of the T. maritima proteome. Representative structures from TM0423 glycerol dehydrogenase and TM0449 thymidylate synthase-complementing protein are presented as examples of final outputs from the pipeline.
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
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Cited by
Protein production and purification
Structural Genomics Consortium, Biologiques, A. E. F. D. M., Berkeley Structural Genomics Center, China Structural Genomics Consortium, Integrated Center for Structure and Function Innovation, Israel Structural Proteomics Center, Joint Center for Structural Genomics, Midwest Center for Structural Genomics, New York Structural GenomiX Research Center for Structural Genomics, Northeast Structural Genomics Consortium, et al. (2008) · Nature Methods · doi:10.1038/nmeth.f.202 · Cited by 916
Brunk, E., & Rothlisberger, U. (2015) · Chemical Reviews · doi:10.1021/cr500628b · Cited by 494
Overview of structural genomics: from structure to function
Zhang, C., & Kim, S.-H. (2003) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00015-7 · Cited by 154
Structural Basis of Substrate Recognition by Hematopoietic Tyrosine Phosphatase,
Critton, D. A., Tortajada, A., Stetson, G., Peti, W., & Page, R. (2008) · Biochemistry · doi:10.1021/bi801724n · Cited by 28
Das, D., Kozbial, P., Han, G. W., Carlton, D., Jaroszewski, L., Abdubek, P., Astakhova, T., Axelrod, H. L., Bakolitsa, C., Chen, C., et al. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309109018168 · Cited by 2
Self-citation
Metadata
- Authors
- Lesley, S. A., Kuhn, P., Godzik, A., Deacon, A. M., Mathews, I., Kreusch, A., Spraggon, G., Klock, H. E., McMullan, D., Shin, T., Vincent, J., Robb, A., Brinen, L. S., Miller, M. D., McPhillips, T. M., Miller, M. A., Scheibe, D., Canaves, J. M., Guda, C., Jaroszewski, L., Selby, T. L., Elsliger, M.-A., Wooley, J., Taylor, S. S., Hodgson, K. O., Wilson, I. A., Schultz, P. G., & Stevens, R. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-08-22
- Volume
- 99
- Issue
- 18
- Pages
- 11664-11669
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2117239890
- Cited by
- 377
- References
- 1
- FWCI
- 28.31
- 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: Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. https://app.cochat.ai/papers/10.1073/pnas.142413399
- The paper
- Lesley, S. A., Kuhn, P., Godzik, A., Deacon, A. M., Mathews, I., Kreusch, A., Spraggon, G., Klock, H. E., McMullan, D., Shin, T., Vincent, J., Robb, A., Brinen, L. S., Miller, M. D., McPhillips, T. M., Miller, M. A., Scheibe, D., Canaves, J. M., Guda, C., . . . Stevens, R. C. (2002). Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.142413399
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.