Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407

Authors: Hu, Hongyan; Wang, Ganggang; Yang, Haitao; Zhou, Ju; Mo, Lijuan; Yang, Kailin; Jin, Chunsheng; Jin, Cheng; Rao, Zihe

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 939-940(2)

Publisher: Blackwell Publishing

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Abstract:

Chitinase hydrolyzes chitin, a linear polymer of β-1,4-linked N-acetylglucosamine (NAG), and plays a variety of roles in the biological world. In addition to endo- and exo-hydrolytic activities, transglycosyl activity has also been observed in the extracellular chitinase (afCHI) from the airborne saprophytic fungi Aspergillus fumigatus YJ-407. Crystals of this native chitinase have been grown at 291 K using PEG 3350 as a precipitant. The diffraction data from the crystal extend to 1.7 Å resolution at BSRF, China. The crystal belongs to space group P2₁2₁2₁, with unit-cell parameters a = 95.7, b = 100.5, c = 134.3 Å. The presence of two molecules per asymmetric unit gives a crystal volume per protein mass (V_M) of 3.6 Å³ Da⁻¹ and a solvent content of 65% by volume. A full set of X-ray diffraction data was collected to 2.1 Å resolution.

Keywords: chitinase

Document Type: Research article

DOI: 10.1107/S0907444904005190

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