ArticleActa crystallographica. Section D, Biological crystallography2009
Effects of impurities on membrane-protein crystallization in different systems.
Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
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- Tracing transport of protein aggregates in microgravity versus unit gravity crystallization.NPJ microgravity · 2022Article
- Heat treatment of thioredoxin fusions increases the purity of α-helical transmembrane protein constructs.Protein science : a publication of the Protein Society · 2021Article
- Heterologous Expression and Biochemical Characterization of the Human Zinc Transporter 1 (ZnT1) and Its Soluble C-Terminal Domain.Frontiers in chemistry · 2021Article
- Article
- First attempts to crystallize a non-homogeneous sample of thioredoxin fromBiochemistry and biophysics reports · 2016Article
- Uncovering the lipidic basis for the preparation of functional nicotinic acetylcholine receptor detergent complexes for structural studies.Scientific reports · 2016Article
- Microgravity protein crystallization.NPJ microgravity · 2015Review
- Crystallization of proteins from crude bovine rod outer segments.Methods in enzymology · 2015Article
- Large-scale production and protein engineering of G protein-coupled receptors for structural studies.Frontiers in pharmacology · 2015Review
- Femtosecond crystallography of membrane proteins in the lipidic cubic phase.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.PloS one · 2012Article
- Lipidic cubic phase technologies for membrane protein structural studies.Current opinion in structural biology · 2011Review
- Monoolein lipid phases as incorporation and enrichment materials for membrane protein crystallization.PloS one · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
When starting a protein-crystallization project, scientists are faced with several unknowns. Amongst them are these questions: (i) is the purity of the starting material sufficient? and (ii) which type of crystallization experiment is the most promising to conduct? The difficulty in purifying active membrane-protein samples for crystallization trials and the high costs associated with producing such samples require an extremely pragmatic approach. Additionally, practical guidelines are needed to increase the efficiency of membrane-protein crystallization. In order to address these conundrums, the effects of commonly encountered impurities on various membrane-protein crystallization regimes have been investigated and it was found that the lipidic cubic phase (LCP) based crystallization methodology is more robust than crystallization in detergent environments using vapor diffusion or microbatch approaches in its ability to tolerate contamination in the forms of protein, lipid or other general membrane components. LCP-based crystallizations produced crystals of the photosynthetic reaction center (RC) of Rhodobacter sphaeroides from samples with substantial levels of residual impurities. Crystals were obtained with protein contamination levels of up to 50% and the addition of lipid material and membrane fragments to pure samples of RC had little effect on the number or on the quality of crystals obtained in LCP-based crystallization screens. If generally applicable, this tolerance for impurities may avoid the need for samples of ultrahigh purity when undertaking initial crystallization screening trials to determine preliminary crystallization conditions that can be optimized for a given target protein.
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