Journal article
Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407
Acta crystallographica. Section D, Biological crystallography, Vol.60(Pt 5), pp.939-940
05/2004
DOI: 10.1107/S0907444904005190
PMID: 15103145
Abstract
Chitinase hydrolyzes chitin, a linear polymer of beta-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 A resolution at BSRF, China. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 95.7, b = 100.5, c = 134.3 A. The presence of two molecules per asymmetric unit gives a crystal volume per protein mass (V(M)) of 3.6 A(3) Da(-1) and a solvent content of 65% by volume. A full set of X-ray diffraction data was collected to 2.1 A resolution.
Details
- Title: Subtitle
- Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407
- Creators
- Hongyan Hu - Microbiology Institute of ShaanxiGanggang Wang - Tsinghua UniversityHaitao Yang - Tsinghua UniversityJu Zhou - Microbiology Institute of ShaanxiLijuan Mo - Tsinghua UniversityKailin Yang - Tsinghua UniversityChunsheng Jin - Microbiology Institute of ShaanxiCheng Jin - Microbiology Institute of ShaanxiZihe Rao - Tsinghua University
- Resource Type
- Journal article
- Publication Details
- Acta crystallographica. Section D, Biological crystallography, Vol.60(Pt 5), pp.939-940
- DOI
- 10.1107/S0907444904005190
- PMID
- 15103145
- ISSN
- 0907-4449
- eISSN
- 1399-0047
- Language
- English
- Date published
- 05/2004
- Academic Unit
- Radiation Oncology
- Record Identifier
- 9984696717402771
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