Russian Journal of Bioorganic Chemistry

, Volume 38, Issue 1, pp 83–88 | Cite as

A novel approach to studying the structural and functional properties of proteins with unknown functions

  • M. A. Gorbacheva
  • A. G. Yarosh
  • P. V. Dorovatovskii
  • T. V. Rakitina
  • K. M. Boiko
  • D. A. Korzhenevskii
  • A. V. Lipkin
  • V. O. Popov
  • I. A. Shumilin
Article
  • 57 Downloads

Abstract

Three proteins from extremophilic bacteria—hypothetical monooxygenase from Deinococcus radiodurans, hypothetical nucleotidyl transferase from Thermotoga maritime, and hypothetical oxidoreductase from Exiguobacterium sibiricum—and the DJ-1 chaperone protein from Homo sapiens have been produced in Escherichia coli. The isolation and purification procedures developed for the recombinant proteins allowed us to achieve yields higher than 96%. Crystallization conditions enabling stable growth of crystals have been determined. X-ray experiments have been performed to test the quality of the crystals and the resolution achieved ranged from 1.2 to 1.8 Å.

Keywords

unknown ligands crystallization X-ray structure analysis 

Abbreviations

MPD

2-methyl-2,4-pentanediol

PEG

polyethylene glycol

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Copyright information

© Pleiades Publishing, Ltd. 2012

Authors and Affiliations

  • M. A. Gorbacheva
    • 1
    • 2
  • A. G. Yarosh
    • 1
  • P. V. Dorovatovskii
    • 1
  • T. V. Rakitina
    • 1
    • 3
  • K. M. Boiko
    • 1
    • 2
  • D. A. Korzhenevskii
    • 1
  • A. V. Lipkin
    • 1
  • V. O. Popov
    • 2
  • I. A. Shumilin
    • 4
  1. 1.Research Center “Kurchatov Institute”MoscowRussia
  2. 2.Bakh Institute of BiochemistryMoscowRussia
  3. 3.Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesMoscowRussia
  4. 4.Virginia UniversityCharlottesvilleUSA

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