Purification, crystallization and preliminary X-ray studies of AxCesD required for efficient cellulose biosynthesis in Acetobacter xylinum

Protein Pept Lett. 2008;15(1):115-7. doi: 10.2174/092986608783330422.

Abstract

AxCesD protein required for bacterial cellulose biosynthesis in Acetobacter xylinum was overexpressed in E. coli, purified and crystallized. Single crystals of SeMet-substituted AxCesD were obtained by the sitting-drop vapor-diffusion method. The crystal belongs to the primitive trigonal space group P3 2, with unit-cell parameters a = b = 77.7 A, and c = 213.9 A. The asymmetric unit in the crystal was assumed to contain 8 protein molecules giving the Matthews coefficient (VM) of 2.54 A3 Da(-1). Se-MAD data were collected to 2.3 A resolution using synchrotron radiations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification*
  • Cellulose / biosynthesis*
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Gluconacetobacter xylinus / chemistry*
  • Gluconacetobacter xylinus / metabolism

Substances

  • Bacterial Proteins
  • Cellulose