Crystallization and preliminary X-ray crystallographic analysis of alginate lyase A1-II from Sphingomonas species A1

Biochim Biophys Acta. 2000 Feb 9;1476(2):382-5. doi: 10.1016/s0167-4838(99)00244-7.

Abstract

Alginate lyase A1-II of Sphingomonas species A1 was purified and crystallized using the hanging drop vapor-diffusion method in 0.1 M Tris-HCl buffer containing 43% saturated ammonium sulfate, 8% polyethylene glycol 4000 and 0.2 M Li(2)SO(4) at pH 8.5 and 20 degrees C. The crystals are tetragonal and belong to the space group P4(3)2(1)2 or P4(1)2(1)2 with unit cell dimensions of a=b=144.07 and c=296.38 A. The diffraction data up to 2.8 A were collected by a synchrotron radiation source at SPring-8 in Japan.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Polysaccharide-Lyases / chemistry*
  • Polysaccharide-Lyases / metabolism
  • Protein Conformation
  • Sphingomonas / chemistry*
  • Sphingomonas / enzymology

Substances

  • Bacterial Proteins
  • Polysaccharide-Lyases
  • poly(beta-D-mannuronate) lyase