Crystallization and preliminary X-ray analysis of class II fructose-1,6-bisphosphate aldolase from Thermus caldophilus

Protein Pept Lett. 2003 Oct;10(5):511-5. doi: 10.2174/0929866033478735.

Abstract

In this study, we have crystallized class II fructose-1,6-bisphosphate aldolase (FBA) from Thermus caldophilus (Tca). Purified Tca FBA is a tetrameric enzyme of 305 residues, which crystallizes in the space group P2(1)2(1)2(1) (cell dimensions a = 98.9, b = 113.1, c = 115.7 A), with four molecules in the asymmetric unit. A complete diffraction data set was obtained from orthorhombic crystals at resolution of 2.2 A.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Crystallography, X-Ray / statistics & numerical data
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Fructose-Bisphosphate Aldolase / chemistry*
  • Fructose-Bisphosphate Aldolase / genetics
  • Fructose-Bisphosphate Aldolase / isolation & purification
  • Molecular Sequence Data
  • Recombinant Proteins / chemistry
  • Sequence Alignment
  • Thermus / enzymology*

Substances

  • Recombinant Proteins
  • Fructose-Bisphosphate Aldolase