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 | |
| 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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