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Crystallization of membrane proteins
Open accessAbstract
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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Cited by
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Rückert, M., & Otting, G. (2000) · Journal of the American Chemical Society · doi:10.1021/ja001068h · Cited by 632
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Kobilka, B. K. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.10.021 · Cited by 623
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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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