Protein L mutants for the crystallization of antibody fragments

Stura, Enrico A., Graille, Marc, Housden, Nicholas G. and Gore, Michael G. (2002) Protein L mutants for the crystallization of antibody fragments Acta Crystallographica Section D: Biological Crystallography, 58, (10-1), pp. 1744-1748. (doi:10.1107/S0907444902012805).


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In many cases, antibody and their complexes can be crystallized and their structure determined without major difficulties. The remaining problematic cases may be approached through techniques such as of combinatorial complex crystallization which uses immunoglobulin binding proteins (IBP). The range of lattices that can be made using this method can be expanded by engineering mutants of IBP domains. We have designed Peptostreptococcus magnus protein L (PpL) mutants with altered immunoglobulin light chain binding characteristics. While the wild type PpL has two binding sites, some of the mutants contact the light chain via only one site. Other mutants have combinations of weakened first and second binding sites that modify their crystallization properties and their packing mode. In this study, we have selected PpL mutants with different behavior and that are most useful for crystallization and we present the various packing modes obtained so far.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1107/S0907444902012805
ISSNs: 0907-4449 (print)
Related URLs:
Keywords: antibody crystallization, immunoglobulin binding protein, crystal engineering, protein L mutants
ePrint ID: 55914
Date :
Date Event
1 October 2002Published
Date Deposited: 06 Aug 2008
Last Modified: 16 Apr 2017 17:42
Further Information:Google Scholar

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