Chitinase is necessary for fungal growth and cell division and, therefore, is an ideal target for the design of inhibitors which may act as antifungal agents. A chitinase from the fungal pathogen Coccidioides immitis has been expressed as a fusion protein with gluathione-S-transferase (GST), which aids in purification. After cleavage from GST, chitinase was crystallized from 30% PEG 4000 in 0.1 M sodium acetate pH 4.6. The crystals have a tetragonal crystal lattice and belong to space group P41212 or P43212 and diffract to 2.2 Å resolution. The unit-cell parameters are a = b = 91.2, c = 95.4 Å; there is only one chitinase molecule in the asymmetric unit.
|Original language||English (US)|
|Number of pages||2|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Issue number||6 PART II|
|State||Published - 1998|
ASJC Scopus subject areas
- Structural Biology