Crystallization and preliminary crystallographic studies of ribulose 1,5-bisphosphate carboxylase/oxygenase from a red alga, Galdieria partita, with a high specificity factor

J Biochem. 1996 Dec;120(6):1064-6. doi: 10.1093/oxfordjournals.jbchem.a021520.

Abstract

Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) from a red alga, Galdieria partita, has been crystallized by the hanging drop vapor diffusion method. Two forms (Forms I and II) of crystals were obtained under distinct conditions. The Form I crystal belongs to monoclinic space group C2 with cell dimensions of a = 190.2, b = 140.0, c = 189.0 A, and beta = 102.6 degrees, and diffracts up to 3.0 A resolution. Diffraction from the Form II crystal was too weak to determine crystal data.

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Protein Conformation
  • Rhodophyta
  • Ribulose-Bisphosphate Carboxylase / chemistry*

Substances

  • Ribulose-Bisphosphate Carboxylase