Engineering of recombinant crystallization chaperones

Curr Opin Struct Biol. 2009 Aug;19(4):449-57. doi: 10.1016/j.sbi.2009.04.008. Epub 2009 May 26.

Abstract

The preparation of diffraction quality crystals remains the major bottleneck in macromolecular X-ray crystallography. A crystallization chaperone is an auxiliary protein, such as fragments of monoclonal antibodies, that binds to and increases the crystallization probability of a target molecule of interest. Such chaperones reduce conformational heterogeneity, mask counterproductive surfaces while extending surfaces predisposed to forming crystal contacts, and provide phasing information. Crystallization chaperones generated using recombinant technologies have emerged as superior alternatives that increase the throughput and eliminate inherent limitations associated with antibody production by animal immunization and the hybridoma technology.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Antibodies / metabolism
  • Crystallization
  • Humans
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / genetics*
  • Molecular Chaperones / metabolism*
  • Protein Engineering / methods*
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics*
  • Recombinant Proteins / metabolism*

Substances

  • Antibodies
  • Molecular Chaperones
  • Recombinant Proteins