We are analyzing https://link.springer.com/protocol/10.1007/978-1-0716-0373-4_19.

Title:
Stabilization and Crystallization of a Membrane Protein Involved in Lipid Transport | SpringerLink
Description:
Lipoteichoic acids (LTA) are ubiquitous cell wall components of Gram-positive bacteria. In Staphylococcus aureus LTA are composed of a polymer with 1,3-linked glycerol phosphate repeating units anchored to the plasma membrane. The anchor molecule is a lipid-linked...
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Keywords {🔍}

pubmed, article, google, scholar, cas, lipoteichoic, acid, membrane, staphylococcus, aureus, wall, biol, protocol, acids, microbiol, central, basel, data, purification, biology, lipid, perez, cell, teichoic, wang, httpsdoiorgs, privacy, cookies, content, information, publish, proteins, protein, grampositive, bacteria, ltaa, structure, crystallography, synthesis, mol, panepucci, springer, analysis, search, expression, structural, stabilization, zhang, camilo, methods,

Topics {✒️}

month download article/chapter d-alanyl-teichoic acids d-alanyl-lipoteichoic acid swiss light source wojdyla ja wall teichoic acid wall teichoic acids lipoteichoic acid synthesis gram-positive bacteria privacy choices/manage cookies lipoteichoic acid polymers lipoteichoic acid carrier device instant download cell wall density huang cy membrane protein involved lta synthesis proteins lipid-linked disaccharide automated data collection cell division machinery springer nature situ serial crystallography characterizing protein crystals serial synchrotron crystallography european economic area highlight key points balancing act times neuhaus fc tagged tev protease improving diffraction quality author information authors editor information editors da+ data acquisition conditions privacy policy disaccharide synthase lpxb structure-based mechanism journal finder publish accepting optional cookies hydrophobic interaction chromatography staphylococcus aureus rn4220 staphylococcus aureus ltas obtain ltaa crystals lipoteichoic acid camilo perez macromolecular crystallography cell wall lipid transport protocol main content log post-crystallization treatments lipoteichoic acids

Schema {🗺️}

ScholarlyArticle:
      headline:Stabilization and Crystallization of a Membrane Protein Involved in Lipid Transport
      pageEnd:292
      pageStart:283
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-0716-0373-4.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Expression, Purification, and Structural Biology of Membrane Proteins
         isbn:
            978-1-0716-0373-4
            978-1-0716-0372-7
         type:Book
      publisher:
         name:Springer US
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Bing Zhang
            affiliation:
                  name:University of Basel
                  address:
                     name:Biozentrum, University of Basel, Basel, Switzerland
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Camilo Perez
            affiliation:
                  name:University of Basel
                  address:
                     name:Biozentrum, University of Basel, Basel, Switzerland
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Membrane protein, Lipid flippases, X-ray crystallography, In situ annealing, TEV protease, Protein purification, Detergent micelles
      description:Lipoteichoic acids (LTA) are ubiquitous cell wall components of Gram-positive bacteria. In Staphylococcus aureus LTA are composed of a polymer with 1,3-linked glycerol phosphate repeating units anchored to the plasma membrane. The anchor molecule is a lipid-linked disaccharide (anchor-LLD) synthesized at the cytoplasmic leaflet of the membrane. The anchor lipid becomes accessible at the outer leaflet of the membrane after the flippase LtaA catalyzes translocation. Recently we have elucidated the structure of LtaA using vapor diffusion X-ray crystallography and in situ annealing. We were able to obtain LtaA crystals after optimization of purification protocols that led to stabilization of LtaA isolated in detergent micelles. Here we report a protocol that describes the purification, stabilization, crystallization, and data collection strategies carried out to determine the structure of LtaA. We highlight key points that can be used to determine crystal structures of other membrane proteins.
      datePublished:2020
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Book:
      name:Expression, Purification, and Structural Biology of Membrane Proteins
      isbn:
         978-1-0716-0373-4
         978-1-0716-0372-7
Organization:
      name:Springer US
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Basel
      address:
         name:Biozentrum, University of Basel, Basel, Switzerland
         type:PostalAddress
      name:University of Basel
      address:
         name:Biozentrum, University of Basel, Basel, Switzerland
         type:PostalAddress
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Person:
      name:Bing Zhang
      affiliation:
            name:University of Basel
            address:
               name:Biozentrum, University of Basel, Basel, Switzerland
               type:PostalAddress
            type:Organization
      name:Camilo Perez
      affiliation:
            name:University of Basel
            address:
               name:Biozentrum, University of Basel, Basel, Switzerland
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Biozentrum, University of Basel, Basel, Switzerland
      name:Biozentrum, University of Basel, Basel, Switzerland
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