The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Entropy and surface engineering in protein crystallization
Open accessAbstract
Protein crystallization remains a key limiting step in the characterization of the atomic structures of proteins and their complexes by X-ray diffraction methods. Current data indicate that standard screening procedures applied to soluble well folded prokaryotic proteins yield X-ray diffraction crystals with an approximately 20% success rate and for eukaryotic proteins this figure may be significantly lower. Protein crystallization is predominantly dependent on entropic effects and the driving force appears to be the release of ordered water from the sites of crystal contacts. This is countered by the entropic cost of ordering of protein molecules and by the loss of conformational freedom of side chains involved in the crystal contacts. Mutational surface engineering designed to create patches with low conformational entropy and thereby conducive to formation of crystal contacts promises to be an effective tool allowing direct enhancement of the success rate of macromolecular crystallization.
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
Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
Lawson, D. M., Artymiuk, P. J., Yewdall, S. J., Smith, J. M. A., Livingstone, J. C., Treffry, A., Luzzago, A., Levi, S., Arosio, P., Cesareni, G., et al. (1991) · Nature · doi:10.1038/349541a0 · Cited by 777
Cited by
Protein crystallization: from purified protein to diffraction-quality crystal
Chayen, N. E., & Saridakis, E. (2008) · Nature Methods · doi:10.1038/nmeth.f.203 · Cited by 390
Zhu, J., Avakyan, N., Kakkis, A., Hoffnagle, A. M., Han, K., Li, Y., Zhang, Z., Choi, T. S., Na, Y., Yu, C.-J., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00308 · Cited by 285
Lysine Methylation as a Routine Rescue Strategy for Protein Crystallization
Walter, T. S., Meier, C., Assenberg, R., Au, K.-F., Ren, J., Verma, A., Nettleship, J. E., Owens, R. J., Stuart, D. I., & Grimes, J. M. (2006) · Structure · doi:10.1016/j.str.2006.09.005 · Cited by 270
He, X., Lobsiger, J., & Stocker, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907454106 · Cited by 73
Nawarathnage, S., Tseng, Y. J., Soleimani, S., Smith, T., Pedroza Romo, M. J., Abiodun, W. O., Egbert, C. M., Madhusanka, D., Bunn, D., Woods, B., et al. (2023) · Structure · doi:10.1016/j.str.2023.09.001 · Cited by 6
Metadata
- Authors
- Derewenda, Z. S., & Vekilov, P. G.
- Venue
- Acta Crystallographica Section D Biological Crystallography
- Published
- 2005-12-14
- Volume
- 62
- Issue
- 1
- Pages
- 116-124
- ISSN
- 0907-4449 (ISSN-L)
- OpenAlex
- W2166033246
- Cited by
- 240
- References
- 1
- FWCI
- 6.65
- Type
- journal article
- Language
- en
- Open access
- hybrid
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: Entropy and surface engineering in protein crystallization. https://app.cochat.ai/papers/10.1107/s0907444905035237
- The paper
- Derewenda, Z. S., & Vekilov, P. G. (2006). Entropy and surface engineering in protein crystallization. Acta Crystallographica Section D Biological Crystallography. https://doi.org/10.1107/s0907444905035237
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.
