ArticleJournal of structural and functional genomics2010
An automated pipeline to screen membrane protein 2D crystallization.
Article in Journal of structural and functional genomics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Drug target mining and in silico screening of Tibetan plant metabolites for potential alleviation of Oroya fever, a neglected tropical disease.Scientific reports · 2026Article
- Zinc binding alters the conformational dynamics and drives the transport cycle of the cation diffusion facilitator YiiP.The Journal of general physiology · 2021Article
- A pipeline approach to single-particle processing in RELION.Acta crystallographica. Section D, Structural biology · 2017Article
- Structure of the SLC4 transporter Bor1p in an inward-facing conformation.Protein science : a publication of the Protein Society · 2017Article
- Sparse and incomplete factorial matrices to screen membrane protein 2D crystallization.Journal of structural biology · 2015Article
- Two-Dimensional Crystallization Procedure, from Protein Expression to Sample Preparation.BioMed research international · 2015Review
- Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- High-throughput methods for electron crystallography.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Membrane protein structure determination by electron crystallography.Current opinion in structural biology · 2012Review
- Electron crystallography--the waking beauty of structural biology.Current opinion in structural biology · 2012Review
- Advances in structural and functional analysis of membrane proteins by electron crystallography.Structure (London, England : 1993) · 2011Review
- Automated electron microscopy for evaluating two-dimensional crystallization of membrane proteins.Journal of structural biology · 2010Article
- Present and future of membrane protein structure determination by electron crystallography.Advances in protein chemistry and structural biology · 2010Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Electron crystallography relies on electron cryomicroscopy of two-dimensional (2D) crystals and is particularly well suited for studying the structure of membrane proteins in their native lipid bilayer environment. To obtain 2D crystals from purified membrane proteins, the detergent in a protein-lipid-detergent ternary mixture must be removed, generally by dialysis, under conditions favoring reconstitution into proteoliposomes and formation of well-ordered lattices. To identify these conditions a wide range of parameters such as pH, lipid composition, lipid-to-protein ratio, ionic strength and ligands must be screened in a procedure involving four steps: crystallization, specimen preparation for electron microscopy, image acquisition, and evaluation. Traditionally, these steps have been carried out manually and, as a result, the scope of 2D crystallization trials has been limited. We have therefore developed an automated pipeline to screen the formation of 2D crystals. We employed a 96-well dialysis block for reconstitution of the target protein over a wide range of conditions designed to promote crystallization. A 96-position magnetic platform and a liquid handling robot were used to prepare negatively stained specimens in parallel. Robotic grid insertion into the electron microscope and computerized image acquisition ensures rapid evaluation of the crystallization screen. To date, 38 2D crystallization screens have been conducted for 15 different membrane proteins, totaling over 3000 individual crystallization experiments. Three of these proteins have yielded diffracting 2D crystals. Our automated pipeline outperforms traditional 2D crystallization methods in terms of throughput and reproducibility.
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