ReviewJournal of bioenergetics and biomembranes1996
Engineering the lac permease for purification and crystallization.
Review in Journal of bioenergetics and biomembranes, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 34 citations in OpenAlex.
- Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes.Biochemistry · 2012Article
- Antibody fragments as tools in crystallography.Clinical and experimental immunology · 2011Review
- Discovery of new GPCR biology: one receptor structure at a time.Structure (London, England : 1993) · 2009Review
- Crystal structures of fusion proteins with large-affinity tags.Protein science : a publication of the Protein Society · 2003Review
- Topology of polytopic membrane protein subdomains is dictated by membrane phospholipid composition.The EMBO journal · 2002Article
- A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition.The EMBO journal · 2002Article
- The central cytoplasmic loop of the major facilitator superfamily of transport proteins governs efficient membrane insertion.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Mesoscopic surfactant organization and membrane protein crystallization.Protein science : a publication of the Protein Society · 2000Article
- Toward the bilayer proteome, electrospray ionization-mass spectrometry of large, intact transmembrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lactose permease is being used as a model system for the rational redesign of a membrane protein with the goal of increasing the likelihood of crystallization. Various modifications to the protein have been added for the purposes of purification, stability, and potential for crystallization. The addition of six consecutive histidines at the C-terminus of the protein allows for rapid purification by nickel-chelate chromatography, and the insertion of an entire protein domain into one of the inner cytoplasmic loops of the permease gives the resulting protein a larger hydrophilic surface area. The increase in polar surface area makes the fusion protein easier to handle and more likely to crystallize. In particular, the introduction of cytochrome b562 of E. coli into the central hydrophilic domain the lac permease results in a fusion protein with the transport activity of the permease and the visible absorbance spectrum of the cytochrome. The "red permease" is very easy to monitor through the steps of expression, purification, concentration, and crystallization.
Indexed as
Identifiers
8786234W2009055581What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.