ArticleNature protocols2009
A general protocol for the crystallization of membrane proteins for X-ray structural investigation.
Article in Nature protocols, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 114 citations in OpenAlex.
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- An improved fluorescent tag and its nanobodies for membrane protein expression, stability assay, and purification.Communications biology · 2020Article
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Production of Recombinant Transmembrane Proteins from Mammalian Cells for Biochemical and Structural Analyses.Current protocols in cell biology · 2020Article
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- Improving the Identification and Coverage of Plant Transmembrane Proteins inFrontiers in plant science · 2020Article
- Expression, Purification, and Crystallization of Full-Length HSV-1 gB for Structure Determination.Methods in molecular biology (Clifton, N.J.) · 2020Article
- DABs are inorganic carbon pumps found throughout prokaryotic phyla.Nature microbiology · 2019Article
- High-throughput stability screening for detergent-solubilized membrane proteins.Scientific reports · 2019Article
- Bacterial phosphoglycosyl transferases: initiators of glycan biosynthesis at the membrane interface.Glycobiology · 2017Review
- Single amino acid substitutions in the selectivity filter render NbXIP1;1α aquaporin water permeable.BMC plant biology · 2017Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Protein crystallography is used to generate atomic resolution structures of protein molecules. These structures provide information about biological function, mechanism and interaction of a protein with substrates or effectors including DNA, RNA, cofactors or other small molecules, ions and other proteins. This technique can be applied to membrane proteins resident in the membranes of cells. To accomplish this, membrane proteins first need to be either heterologously expressed or purified from a native source. The protein has to be extracted from the lipid membrane with a mild detergent and purified to a stable, homogeneous population that may then be crystallized. Protein crystals are then used for X-ray diffraction to yield atomic resolution structures of the desired membrane protein target. Below, we present a general protocol for the growth of diffraction quality membrane protein crystals. The process of protein crystallization is highly variable, and obtaining diffraction quality crystals can require weeks to months or even years in some cases.
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