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Cited by 303

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

PROTEIN CRYSTALLIZATION

Durbin, S. D., Feher, G.·1996·Annual Review of Physical Chemistry

Abstract

▪ Abstract Crystallization is necessary to obtain the three-dimensional structure of proteins and nucleic acids; it often represents the bottleneck in structure determination. Our understanding of crystallization mechanisms is still incomplete. In this review, we emphasize fundamental aspects of the crystallization process. Protein-protein contacts in crystals are complex, involving a delicate balance of specific and nonspecific interactions. Depending on solution conditions, these interactions can lead to nucleation of crystals or to amorphous aggregation; this stage of crystallization has been successfully studied by light scattering. Post nucleation crystal growth may proceed by mechanisms involving crystal defects or two-dimensional nucleation, as observed by atomic force and interference microscopy. Cessation of growth has been observed but remains incompletely understood. Impurities may play important roles during all stages of crystallization. Phase diagrams can guide optimization of conditions for nucleation and subsequent crystal growth; a theoretical understanding relating these to the intermolecular interactions is beginning to develop.

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Crossref · 10.1146/annurev.physchem.47.1.171

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Metadata

Authors
Durbin, S. D., & Feher, G.
Venue
Annual Review of Physical Chemistry
Published
1996-10
Volume
47
Issue
1
Pages
171-204
ISSN
  • 0066-426X (ISSN-L)
  • 1545-1593
OpenAlex
W4236190433
Cited by
303
References
2
FWCI
1.90
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: PROTEIN CRYSTALLIZATION. https://app.cochat.ai/papers/10.1146/annurev.physchem.47.1.171
The paper
Durbin, S. D., & Feher, G. (1996). PROTEIN CRYSTALLIZATION. Annual Review of Physical Chemistry. https://doi.org/10.1146/annurev.physchem.47.1.171

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.