Expression, purification, crystallization and preliminary X-ray analysis of human argininosuccinic acid lyase

J Mol Biol. 1994 Jun 3;239(2):336-8. doi: 10.1006/jmbi.1994.1372.

Abstract

Human argininosuccinic acid lyase (ASAL) has been expressed, purified and crystallized in several distinct crystal morphologies. At present only one form is suitable for X-ray diffraction analysis. These crystals grow as hexagonal prisms, with unit cell dimensions a = b = 104.6 A, c = 185.3 A and alpha = beta = 90 degrees, gamma = 120 degrees. The crystals exhibit the symmetry of space group P3(1)21 or its enantiomorph, P3(2)21 (indistinguishable crystallographically) and diffract to a minimum d-spacing of approximately 3.5 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Argininosuccinate Lyase / biosynthesis
  • Argininosuccinate Lyase / chemistry*
  • Argininosuccinate Lyase / isolation & purification
  • Crystallization
  • Crystallography, X-Ray / methods
  • Humans
  • Multigene Family
  • Protein Conformation*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • Recombinant Proteins
  • Argininosuccinate Lyase