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High- Throughput Crystallography for Structural Proteomics

  • Jeff Yon
  • Mladen Vinkovic
  • Harren Jhoti

Abstract

The last decade has seen the success of large-scale sequence determination projects, and an increasing number of sequenced genomes have become available (http:// www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Genome). This in turn has led to efforts to understand the functions of the many newly discovered proteins, and hence to greater interest in high-throughput protein structure determination (1,bi2). Thus the last 5 yr has seen the rise of structural proteomics efforts, whose goal has been the large-scale determination of protein structures using the techniques of X-ray crystallography and nuclear magnetic resonance (NMR) (the terms structural proteomics and structural genomics are often used interchangeably, and no distinction is made in this review). Structural proteomics is expected to contribute to functional studies, as the structures of novel proteins may give insight into their functions as well as having a major impact on drug discovery, as some of these new proteins will be therapeutic targets (3,4 ). An additional level of complexity results from the fact that proteins are often found as part of multiprotein complexes. Although high-throughput structure determination of multiprotein complexes will be even more difficult than for isolated proteins, it will undoubtedly lead to a better understanding of function and mechanism (5).

Keywords

Laboratory Information Management System Protein Structure Initiative Image Plate Detector Structural Proteomics Mercuric Salt 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc., Totowa, NJ 2005

Authors and Affiliations

  • Jeff Yon
    • 1
  • Mladen Vinkovic
    • 1
  • Harren Jhoti
    • 1
  1. 1.Astex Technology Ltd.Cambridge

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