Crystallization and preliminary X-ray analysis of a chitinase from the fungal pathogen Coccidioides immitis

Citation
T. Hollis et al., Crystallization and preliminary X-ray analysis of a chitinase from the fungal pathogen Coccidioides immitis, ACT CRYST D, 54, 1998, pp. 1412-1413
Citations number
12
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
54
Year of publication
1998
Part
6
Pages
1412 - 1413
Database
ISI
SICI code
0907-4449(19981101)54:S2<1412:CAPXAO>2.0.ZU;2-4
Abstract
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 a ids in purification. After cleavage from GST, chitinase was crystallized fr om 30% PEG 4000 in 0.1 M sodium acetate pH 4.6. The crystals have a tetrago nal crystal lattice and belong to space group P4(1)2(1)2 or P4(3)2(1)2 and diffract to 2.2 Angstrom resolution. The unit-cell parameters are a = b = 9 1.2, c = 95.4 Angstrom; there is only one chitinase molecule in the asymmet ric unit.