Preliminary crystallographic study of protocatechuate 3,4-Dioxygenase from Brevibacterium fuscum

Cathleen A. Earhart, R. Radhakrishnan, Allen M. Orville, John D. Lipscomb, Douglas H. Ohlendorf

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The enzyme protocatechuate 3,4-dioxygenase from the Gram positive organism Brevibacterium fuscum crystallizes in the triclinic space group P1 with unit cell dimensions a = 96.1 Å, b = 97.2 Å, c = 118.1 Å and α = 113.9°, β = 90.7°, γ = 117.8°. The rod-like crystals diffract to 2.4 Å resolution. Rotation function analysis suggests that there are six protomers arranged with local 32 symmetry in the asymmetric unit rather than the previously proposed pentameric complex.

Original languageEnglish (US)
Pages (from-to)374-376
Number of pages3
JournalJournal of Molecular Biology
Volume236
Issue number1
DOIs
StatePublished - Feb 10 1994

Keywords

  • Brevibacterium fuscum
  • Crystallization
  • Dioxygenase
  • X-ray crystallography

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