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Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals

Research output: Contribution to journalArticlepeer-review

  • P.T. Erskine
  • J. Cooper
  • R. Lambert
  • G. Lewis
  • Professor Steve Wood
  • P.M. Shoolingin-jordan
  • S. Maignan
  • P. Spencer
  • N. Senior
  • S. Awan
  • M. Warren
  • I.J. Tickle
  • P. Thomas
5-Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecules of 5-aminolaevulinic acid. Both Escherichia coli and Saccharomyces cerevisiae ALADs are homo-octameric enzymes which depend on Zn2+ for catalytic activity and are potently inhibited by lead ions. The E. coli enzyme crystallized in space group I422 (unit cell dimensions a = b = 130.7 A, c = 142.4 A). The best crystals were obtained in the presence of the covalently bound inhibitor laevulinic acid. The yeast enzyme (expressed in E. coli) crystallized in the same space group (I422) but with a smaller unit cell volume (a = b = 103.7 A, c = 167.7 A). High resolution synchrotron data sets were obtained from both E. coli and yeast ALAD crystals by cryocooling to 100 K.
Original languageEnglish
Pages (from-to)1774-1776
JournalProtein Science
Issue number8
Publication statusPublished - 1 Aug 1997

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