The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
Open accessAbstract
Understanding the mechanisms of action of membrane proteins requires the elucidation of their structures to high resolution. The critical step in accomplishing this by x-ray crystallography is the routine availability of well-ordered three-dimensional crystals. We have devised a novel, rational approach to meet this goal using quasisolid lipidic cubic phases. This membrane system, consisting of lipid, water, and protein in appropriate proportions, forms a structured, transparent, and complex three-dimensional lipidic array, which is pervaded by an intercommunicating aqueous channel system. Such matrices provide nucleation sites (“seeding”) and support growth by lateral diffusion of protein molecules in the membrane (“feeding”). Bacteriorhodopsin crystals were obtained from bicontinuous cubic phases, but not from micellar systems, implying a critical role of the continuity of the diffusion space (the bilayer) on crystal growth. Hexagonal bacteriorhodopsin crystals diffracted to 3.7 Å resolution, with a space group P6 3 , and unit cell dimensions of a = b = 62 Å, c = 108 Å; α = β = 90° and γ = 120°.
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Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria
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Crystal structures explain functional properties of two E. coli porins
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Self-citationStructures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å
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Electron-crystallographic Refinement of the Structure of Bacteriorhodopsin
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Nicotinic Acetylcholine Receptor an 9 Å Resolution
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High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor
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Structure of bacteriorhodopsin at 1.55 Å resolution
Luecke, H., Schobert, B., Richter, H.-T., Cartailler, J.-P., & Lanyi, J. K. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3027 · Cited by 1,450
Retinylidene Proteins: Structures and Functions from Archaea to Humans
Spudich, J. L., Yang, C.-S., Jung, K.-H., & Spudich, E. N. (2000) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.16.1.365 · Cited by 675
Detergents as Tools in Membrane Biochemistry
Garavito, R. M., & Ferguson-Miller, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100031200 · Cited by 560
Serial Femtosecond Crystallography of G Protein–Coupled Receptors
Liu, W., Wacker, D., Gati, C., Han, G. W., James, D., Wang, D., Nelson, G., Weierstall, U., Katritch, V., Barty, A., et al. (2013) · Science · doi:10.1126/science.1244142 · Cited by 455
Metadata
- Authors
- Landau, E. M., & Rosenbusch, J. P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-12-10
- Volume
- 93
- Issue
- 25
- Pages
- 14532-14535
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2048695489
- Cited by
- 984
- References
- 24
- FWCI
- 20.61
- Type
- journal article
- Language
- en
- Open access
- green
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