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

被引:7
作者
Hollis, T [1 ]
Monzingo, AF
Bortone, K
Schelp, E
Cox, R
Robertus, JD
机构
[1] Univ Texas, Dept Chem & Biochem, Inst Mol & Cellular Biol, Austin, TX 78712 USA
[2] Texas Ctr Infect Dis, Dept Clin Invest, San Antonio, TX 78223 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1998年 / 54卷
关键词
D O I
10.1107/S0907444998008531
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1412 / 1413
页数:2
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