ArticleMethods in molecular biology (Clifton, N.J.)2010
Two-dimensional crystallization of integral membrane proteins for electron crystallography.
Article in Methods in molecular biology (Clifton, N.J.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- Studying membrane proteins with MicroED.Biochemical Society transactions · 2022Article
- A Diazirine-Modified Membrane Lipid to Study Peptide/Lipid Interactions - Chances and Challenges.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
- Sparse and incomplete factorial matrices to screen membrane protein 2D crystallization.Journal of structural biology · 2015Article
- High-throughput methods for electron crystallography.Methods in molecular biology (Clifton, N.J.) · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Although membrane proteins make up 30% of the proteome and are a common target for therapeutic drugs, determination of their atomic structure remains a technical challenge. Electron crystallography represents an alternative to the conventional methods of X-ray diffraction and NMR and relies on the formation of two-dimensional crystals. These crystals are produced by reconstituting purified, detergent-solubilized membrane proteins back into the native environment of a lipid bilayer. This chapter reviews methods for producing two-dimensional crystals and for screening them by negative stain electron microscopy. In addition, we show examples of the different morphologies that are commonly obtained and describe basic image analysis procedures that can be used to evaluate their promise for structure determination by cryoelectron microscopy.
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