Crystallization and preliminary X‐ray analysis of a chitinase from the fungal pathogen Coccidioides immitis
Author(s) -
Hollis Thomas,
Monzingo Arthur F.,
Bortone Kara,
Schelp Elisabeth,
Cox Rebecca,
Robertus Jon D.
Publication year - 1998
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444998008531
Subject(s) - coccidioides immitis , coccidioides , chitinase , pathogen , microbiology and biotechnology , crystallization , fungal pathogen , biology , enzyme , chemistry , biochemistry , organic chemistry
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 P 4 1 2 1 2 or P 4 3 2 1 2 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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom