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

Thomas Hollis, Arthur F. Monzingo, Kara Bortone, Elisabeth Schelf, Rebecca Cox, Jon D. Robertus

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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 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 languageEnglish (US)
Pages (from-to)1412-1413
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number6 PART II
DOIs
StatePublished - 1998
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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