Crystallization And Preliminary X-Ray Analysis Of A Chitinase From The Fungal Pathogen Coccidioides Immitis
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Date
1998-11
Authors
Hollis, Thomas
Monzingo, Arthur F.
Bortone, Kara
Schelp, Elisabeth
Cox, Rebecca
Robertus, Jon D.
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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 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 = 91.2, c = 95.4 Angstrom; there is only one chitinase molecule in the asymmetric unit.
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Hollis, Thomas, Monzingo, Arthur F., Bortone, Kara, Schelp, Elisabeth, Cox, Rebecca, Robertus, Jon D., >Crystallization and preliminary X-ray analysis of a chitinase from the fungal pathogen Coccidioides immitis, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1412-3. doi: 10.1107/S0907444998008531