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Protein biophysical properties that correlate with crystallization success in thermotoga maritima: Maximum clustering strategy for structural genomics

Academic Article
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Overview

authors

  • Canaves, J. M.
  • Page, R.
  • Wilson, Ian
  • Stevens, Raymond

publication date

  • December 2004

journal

  • Journal of Molecular Biology  Journal

abstract

  • Cost and time reduction are two of the driving forces in the development of new strategies for protein crystallization and subsequent structure determination. Here, we report the analysis of the Thermotoga maritima proteome, in which we compare the proteins that were successfully expressed, purified and crystallized versus the rest of the proteome. This set of almost 500 proteins represents one of the largest, internally consistent, protein expression and crystallization datasets available. The analysis shows that individual parameters, such as isoelectric point, sequence length, average hydropathy, low complexity regions (SEG), and combinations of these biophysical properties for crystallized proteins define a distinct subset of the T. maritima proteome. The distribution profiles of the various biophysical properties in the expression/crystallization set are then used to extract rules to improve target selection and improve the efficiency and output of structural genomics, as well as general structural biology efforts.

subject areas

  • Amino Acid Sequence
  • Amino Acids
  • Bacterial Proteins
  • Crystallography, X-Ray
  • Isoelectric Point
  • Open Reading Frames
  • Protein Conformation
  • Protein Sorting Signals
  • Proteome
  • Thermotoga maritima
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Research

keywords

  • crystallization
  • expression
  • protein properties
  • structural genomics
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2004.09.076

PubMed ID

  • 15544807
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Additional Document Info

start page

  • 977

end page

  • 991

volume

  • 344

issue

  • 4

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