ArticleJournal of structural biology2015
Sparse and incomplete factorial matrices to screen membrane protein 2D crystallization.
Article in Journal of structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- A novel small molecule chaperone of rod opsin and its potential therapy for retinal degeneration.Nature communications · 2018Article
- Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure of the SLC4 transporter Bor1p in an inward-facing conformation.Protein science : a publication of the Protein Society · 2017Article
- Deducing the symmetry of helical assemblies: Applications to membrane proteins.Journal of structural biology · 2016Article
- Protein crystallization screens developed at the MRC Laboratory of Molecular Biology.Drug discovery today · 2016Review
- Automated data collection in single particle electron microscopy.Microscopy (Oxford, England) · 2016Review
- In situ X-ray data collection and structure phasing of protein crystals at Structural Biology Center 19-ID.Journal of synchrotron radiation · 2015Article
- Two-Dimensional Crystallization Procedure, from Protein Expression to Sample Preparation.BioMed research international · 2015Review
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Electron crystallography is well suited for studying the structure of membrane proteins in their native lipid bilayer environment. This technique relies on electron cryomicroscopy of two-dimensional (2D) crystals, grown generally by reconstitution of purified membrane proteins into proteoliposomes under conditions favoring the formation of well-ordered lattices. Growing these crystals presents one of the major hurdles in the application of this technique. To identify conditions favoring crystallization a wide range of factors that can lead to a vast matrix of possible reagent combinations must be screened. However, in 2D crystallization these factors have traditionally been surveyed in a relatively limited fashion. To address this problem we carried out a detailed analysis of published 2D crystallization conditions for 12 β-barrel and 138 α-helical membrane proteins. From this analysis we identified the most successful conditions and applied them in the design of new sparse and incomplete factorial matrices to screen membrane protein 2D crystallization. Using these matrices we have run 19 crystallization screens for 16 different membrane proteins totaling over 1300 individual crystallization conditions. Six membrane proteins have yielded diffracting 2D crystals suitable for structure determination, indicating that these new matrices show promise to accelerate the success rate of membrane protein 2D crystallization.
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