Crystallization and preliminary crystallographic analysis of a new crystal form of arylsulfatase A isolated from human placenta

Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):650-2. doi: 10.1107/s0907444900003085.

Abstract

Depending on pH, arylsulfatase A exists in solution as a dimer or as an octamer. The enzyme isolated from human placenta was crystallized at pH 5.4 in a new crystal form with space group C2, unit-cell parameters a = 154.0, b = 190.3, c = 112.5 A, beta = 122.4 degrees and four subunits in the asymmetric unit. At pH 6.5-6.7, tetragonal crystals are obtained that are isomorphous to the known crystals of recombinant arylsulfatase A obtained at pH 5.0-5.4. The crystal structure of both forms was determined by the molecular-replacement method. The monoclinic crystals contain octamers of the same type as found in the tetragonal form.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cerebroside-Sulfatase / chemistry*
  • Cerebroside-Sulfatase / isolation & purification
  • Computer Graphics
  • Crystallization
  • Crystallography, X-Ray / methods
  • Dimerization
  • Female
  • Humans
  • Models, Molecular
  • Placenta / enzymology*
  • Pregnancy
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • Recombinant Proteins
  • Cerebroside-Sulfatase