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  Crystallisation of membrane proteins mediated by antibody fragments [Review]

Hunte, C., & Michel, H. (2002). Crystallisation of membrane proteins mediated by antibody fragments [Review]. Current Opinion in Structural Biology, 12(4), 503-508. doi:10.1016/S0959-440X(02)00354-8.

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 Creators:
Hunte, Carola1, Author           
Michel, Hartmut1, Author                 
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Membranes; membrane proteins; structure determination; antibody fragment; crystallisation; cytochrome c oxidase; cytochrome bc1 complex; potassium channel Biochemistry; Immunology; Structural biology; Techniques & Methods
 Abstract: X-ray structures of three different membrane proteins in complex with antibody fragments have been published. The binding of Fv or Fab fragments enlarges the hydrophilic part of integral membrane proteins, thereby providing additional surface for crystal contacts and space for the detergent micelle. In all reported cases, antibody binding was either essential for the crystallisation of the membrane protein or it substantially improved the diffraction quality of the crystals. Antibody-fragment-mediated crystallisation appears to be a valuable tool in particular for membrane proteins with very small hydrophilic or flexible domains.

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Language(s): eng - English
 Dates: 20022002-08-052002-08-01
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0959-440X(02)00354-8
 Degree: -

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Title: Current Opinion in Structural Biology
  Other : Curr. Opin. Struct. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 12 (4) Sequence Number: - Start / End Page: 503 - 508 Identifier: ISSN: 0959-440X
CoNE: https://pure.mpg.de/cone/journals/resource/954925578067