Crystallization and preliminary X-ray data for the A-isozyme of O-acetylserine sulfhydrylase from Salmonella typhimurium

G. S Jagannatha Rao, James Mottonen, Elizabeth J. Goldsmith, Paul F. Cook

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

The A-isozyme of O-acetylserine sulfhydrylase, a pyridoxal phosphate-dependent enzyme isolated from Salmonella typhimurium catalyzes the synthesis of L-cysteine from O-acetyl-L-serine and sulfide. The pyridoxal form of the enzyme has been crystallized in two different forms. One form is in the orthorhombic space group P212121 with cell constants a = 144.4 Å, b = 96.9 Å and c = 54.3 Å and contains two monomers each of molecular weight 34,000 per asymmetric unit. The second form is in a hexagonal space group with unit cell dimensions a = b = 115 Å, and c = 348 Å and contains two 68,000 dimers per asymmetric unit. Complete native enzyme data sets have been collected for both crystal forms using an R-Axis II detector. A search for suitable heavy-atom derivatives is underway. Although both crystal forms diffract X-rays to better than 2.5 Å, the orthorhombic form is more suited to a detailed structural analysis due to the extended lifetime in the X-ray beam and the relative size of the unit cell.

Original languageEnglish (US)
Pages (from-to)1130-1132
Number of pages3
JournalJournal of Molecular Biology
Volume231
Issue number4
DOIs
StatePublished - Aug 1 1993

Keywords

  • Crystallization
  • O-acetylserine sulfhydrylase
  • Pyridoxal 5′-phosphate
  • Salmonella typhimurium

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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