Purification, crystallization and preliminary X-ray crystallographic analysis of chitinase from Bacillus cereus NCTU2

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt 9):916-9. doi: 10.1107/S1744309106031423. Epub 2006 Aug 26.

Abstract

Chitinases (EC 3.2.1.14) are found in a broad range of organisms, including bacteria, fungi and higher plants, and play different roles depending on their origin. A chitinase from Bacillus cereus NCTU2 (ChiNCTU2) capable of hydrolyzing chitin as a carbon and nitrogen nutrient has been identified as a member of the family 18 glycoside hydrolases. ChiNCTU2 of molecular weight 36 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of chitinase crystals at 1.10 A resolution, the crystal belongs to space group P2(1), with unit-cell parameters a = 50.79, b = 48.79, c = 66.87 A, beta = 99.31 degrees . Preliminary analysis indicates there is one chitinase molecule in the asymmetric unit, with a solvent content of 43.4%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus cereus / enzymology*
  • Bacillus cereus / genetics
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Chitin / chemistry
  • Chitin / metabolism
  • Chitinases / chemistry*
  • Chitinases / genetics
  • Chitinases / isolation & purification
  • Crystallization
  • Crystallography, X-Ray / methods
  • Hydrolysis

Substances

  • Bacterial Proteins
  • Chitin
  • Chitinases