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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Turner, MA; Achyuthan, AM; Hershfield, MS; McInnes, RR; Howell, PL

Published Date

  • June 3, 1994

Published In

Volume / Issue

  • 239 / 2

Start / End Page

  • 336 - 338

PubMed ID

  • 8196062

Pubmed Central ID

  • 8196062

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1994.1372

Language

  • eng

Conference Location

  • England