Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans

Protein Sci. 1995 May;4(5):1007-9. doi: 10.1002/pro.5560040521.

Abstract

Recombinant Aspergillus nidulans isopenicillin N synthase was purified from an Escherichia coli expression system. The apoenzyme in the presence of saturating concentrations of MnCl2 could be crystallized by either macro- or microseeding, using the hanging drop vapor diffusion technique with polyethylene glycol 8000 as precipitant. The crystals (0.5-1.0 mm overall dimensions) diffract X-rays to at least 2.0 A resolution at synchrotrons and belong to space group P212121 with unit cell dimensions of a = 59.2 A, b = 127.0 A, and c = 139.6 A. The asymmetric unit contains one dimer, and the solvent content of the crystals is 60%. The crystals are radiation sensitive.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus nidulans / enzymology
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Structure
  • Oxidoreductases / chemistry*
  • Oxidoreductases / genetics
  • Oxidoreductases / isolation & purification
  • Polyethylene Glycols
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • Recombinant Proteins
  • Polyethylene Glycols
  • Oxidoreductases
  • isopenicillin N synthetase