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Crystallization and Preliminary X-Ray Analysis of the Catalytic Domain of Chitinase D from Bacillus circulans WL-12

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Abstract:

We report here on crystallization and preliminary X-ray analysis of the catalytic domain of chitinase D from Bacillus circulans WL-12. The native crystals of this domain were found to belong to the orthorhombic space group P212121. To elucidate the structure of the catalytic domain by the multiple isomorphous replacement method, 30 kinds of derivatized crystals were prepared by soaking the native crystals into a mother liquor containing salts of heavy metal atoms. Difference Patterson maps calculated for four derivatives showed strong peaks in the Harker sections.





Keywords: Bacillus circulans WL-12; catalytic domain; chitinase D; crystallization; preliminary X-ray analysis

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606778256108

Affiliations: Department of BioEngineering, Nagaoka University of Technology, Kamitomioka, Nagaoka, Niigata 940-2188, Japan.

Publication date: September 1, 2006

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
ben/ppl/2006/00000013/00000009/art00012
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