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Purification, Crystallization and Preliminary X-Ray Studies of AxCesD Required for Efficient Cellulose Biosynthesis in Acetobacter xylinum

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AxCesD protein required for bacterial cellulose biosynthesis in Acetobacter xylinum was overexpressed in E. coli, purified and crystallized. Single crystals of SeMet-substituted AxCesD were obtained by the sitting-drop vapordiffusion method. The crystal belongs to the primitive trigonal space group P32, with unit-cell parameters a = b = 77.7 Å, and c = 213.9 Å. The asymmetric unit in the crystal was assumed to contain 8 protein molecules giving the Matthews coefficient (VM ) of 2.54 Å3 Da-1. Se-MAD data were collected to 2.3 Å resolution using synchrotron radiations.

Keywords: Acetobacter xylinum; AxCesD; bacterial cellulose; biosynthesis; crystal

Document Type: Research Article


Publication date: January 1, 2008

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  • 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.

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