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|Title:||Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae|
Robert C. Robinson
Suranaree University of Technology
National Synchrotron Research Center, Thailand
Institute of Molecular and Cell Biology, A-Star, Singapore
Max Planck Institut fur molekulare Physiologie
|Keywords:||Biochemistry, Genetics and Molecular Biology;Physics and Astronomy|
|Citation:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.61, No.10 (2005), 895-898|
|Abstract:||Chitinase A of Vibrio carchariae was expressed in Escherichia coli M15 host cells as a 575-amino-acid fragment with full enzymatic activity using the pQE60 expression vector. The yield of the highly purified recombinant protein was approximately 70 mg per litre of bacterial culture. The molecular mass of the expressed protein was determined by HPLC/ESI-MS to be 63 770, including the hexahistidine tag. Crystals of recombinant chitinase A were grown to a suitable size for X-ray structure analysis in a precipitant containing 10%(v/v) PEG 400, 0.1 M sodium acetate pH 4.6 and 0.125 M CaCl2. The crystals belonged to the tetragonal space group P422, with two molecules per asymmetric unit and unit-cell parameters a = b = 127.64, c = 171.42 Å. A complete diffraction data set was collected to 2.14 Å resolution using a Rigaku/MSC R-AXIS IV++detector system mounted on an RU-H3R rotating-anode X-ray generator. © 2005 International Union of Crystallography All rights reserved.|
|Appears in Collections:||Scopus 2001-2005|
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