Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography

Alain Brisson; Anders Olofsson; Philippe Ringler; Marc Schmutz; Svetla Stoylova

doi:10.1111/j.1768-322x.1994.tb00933.x

Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography

Alain Brisson, Anders Olofsson, Philippe Ringler, Marc Schmutz, Svetla Stoylova

Research output: Contribution to journal › Article › peer-review

50 Scopus citations

Abstract

Electron crystallography constitutes a powerful new method for determining the struture of biological macromolecules. This method is best adapted to the study of ordered assemblies of macromolecules, and principally to two-dimensional (2-D) crystals of proteins. Obtaining protein 2-D crystals ordered at high resolution constitutes the major limiting step in the application of this approach. Considerable interest has been raised by the development of a rational method of 2-D crystallization based on the specific binding of proteins to planar lipid films. The applicability of this method is quasi-general in the case of soluble proteins. Its basic principles, together with examples taken from work in our group, are presented here.

Original language	English (US)
Pages (from-to)	221-228
Number of pages	8
Journal	Biology of the Cell
Volume	80
Issue number	2-3
DOIs	https://doi.org/10.1111/j.1768-322x.1994.tb00933.x
State	Published - 1994
Externally published	Yes

Keywords

2-D crystals
electron crystallography
membrane-bound proteins
planar lipid films

ASJC Scopus subject areas

Cell Biology

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10.1111/j.1768-322x.1994.tb00933.x

Cite this

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title = "Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography",

abstract = "Electron crystallography constitutes a powerful new method for determining the struture of biological macromolecules. This method is best adapted to the study of ordered assemblies of macromolecules, and principally to two-dimensional (2-D) crystals of proteins. Obtaining protein 2-D crystals ordered at high resolution constitutes the major limiting step in the application of this approach. Considerable interest has been raised by the development of a rational method of 2-D crystallization based on the specific binding of proteins to planar lipid films. The applicability of this method is quasi-general in the case of soluble proteins. Its basic principles, together with examples taken from work in our group, are presented here.",

keywords = "2-D crystals, electron crystallography, membrane-bound proteins, planar lipid films",

author = "Alain Brisson and Anders Olofsson and Philippe Ringler and Marc Schmutz and Svetla Stoylova",

note = "Funding Information: bition of coagulation through a surface-depletion mechanism [7]. This hypothesis has recently been supported by fluorescence spectroscopy experiments [25].",

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doi = "10.1111/j.1768-322x.1994.tb00933.x",

language = "English (US)",

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journal = "Biology of the Cell",

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T1 - Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography

AU - Brisson, Alain

AU - Olofsson, Anders

AU - Ringler, Philippe

AU - Schmutz, Marc

AU - Stoylova, Svetla

N1 - Funding Information: bition of coagulation through a surface-depletion mechanism [7]. This hypothesis has recently been supported by fluorescence spectroscopy experiments [25].

PY - 1994

Y1 - 1994

N2 - Electron crystallography constitutes a powerful new method for determining the struture of biological macromolecules. This method is best adapted to the study of ordered assemblies of macromolecules, and principally to two-dimensional (2-D) crystals of proteins. Obtaining protein 2-D crystals ordered at high resolution constitutes the major limiting step in the application of this approach. Considerable interest has been raised by the development of a rational method of 2-D crystallization based on the specific binding of proteins to planar lipid films. The applicability of this method is quasi-general in the case of soluble proteins. Its basic principles, together with examples taken from work in our group, are presented here.

AB - Electron crystallography constitutes a powerful new method for determining the struture of biological macromolecules. This method is best adapted to the study of ordered assemblies of macromolecules, and principally to two-dimensional (2-D) crystals of proteins. Obtaining protein 2-D crystals ordered at high resolution constitutes the major limiting step in the application of this approach. Considerable interest has been raised by the development of a rational method of 2-D crystallization based on the specific binding of proteins to planar lipid films. The applicability of this method is quasi-general in the case of soluble proteins. Its basic principles, together with examples taken from work in our group, are presented here.

KW - 2-D crystals

KW - electron crystallography

KW - membrane-bound proteins

KW - planar lipid films

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Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography

Abstract

Keywords

ASJC Scopus subject areas

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