Crystallization and preliminary X-ray diffraction studies of Streptomyces phospholipase A2 in a calcium-binding form

J Inorg Biochem. 2000 Nov;82(1-4):221-3. doi: 10.1016/s0162-0134(00)00147-1.

Abstract

Phospholipase A2 (PLA2) as a calcium-binding form, produced by Streptomyces violaceoruber, was crystallized in a form suitable for the diffraction analysis using the vapor diffusion method. Crystals were grown in 0.1 M Tris-HCl buffer (pH 8.5), 20 mM Ca2+ containing 50-60% (v/v) 2-methyl-2,4-pentanediol as a precipitant. They belong to the monoclinic space group P2(1), with the cell dimensions a=38.3 A, b=54.3 A, c=30.6 A, and beta=90.2 degrees. The crystals diffract the X-ray well and the diffraction intensity data were collected up to 1.6 A resolution. The crystal volume per unit mass, V(M) is 2.35 A3 Da(-1) with one molecule in the asymmetric unit, which corresponds to a solvent content of 47.7%.

MeSH terms

  • Calcium / metabolism
  • Crystallization
  • Phospholipases A / chemistry*
  • Phospholipases A / metabolism
  • Phospholipases A2
  • Streptomyces / enzymology*
  • X-Ray Diffraction

Substances

  • Phospholipases A
  • Phospholipases A2
  • Calcium