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Crystallization of membrane proteins

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Ostermeier, Christian, Michel, Hartmut·1997·Current Opinion in Structural Biology

Abstract

Five new membrane protein structures have been determined since 1995 using X-ray crystallography: bacterial light-harvesting complex; bacterial and mitochondrial cytochrome c oxidases; mitochondrial bc1 complex; and alpha-hemolysin. These successes are partly based on advances in the crystallization procedures for integral membrane proteins. Variation of the size of the detergent micelle and/or increasing the size of the polar surface of the membrane protein is the most important route to well-ordered membrane protein crystals. The use of bicontinuous lipidic cubic phases also appears to be promising.

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Metadata

Authors
Ostermeier, C., & Michel, H.
Venue
Current Opinion in Structural Biology
Publisher
Elsevier BV
Published
1997-10
Volume
7
Issue
5
Pages
697-701
ISSN
0959-440X (ISSN-L)
OpenAlex
W2101327053
Cited by
439
References
0
FWCI
5.00
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Crystallization of membrane proteins. https://app.cochat.ai/papers/10.1016/s0959-440x(97)80080-2
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Ostermeier, C., & Michel, H. (1997). Crystallization of membrane proteins. Current Opinion in Structural Biology. https://doi.org/10.1016/s0959-440x(97)80080-2

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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.