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Crystallization and Preliminary X-Ray Analysis of Sau3AI/E64A Mutant Protein

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Sau3AI is a type II restriction endonuclease that recognizes the palindromic sequence 5’-GATC-3’ and cleaves 5’ to G residue on each strand. The E64A mutant full length protein was cloned and expressed in Escherichia coli. The purified (His)6-tagged protein has monomer and dimer fraction and was crystallized by the hanging-drop vapor-diffusion technique. The dimer protein crystals can diffract to 3.0Å resolution and the monomer protein crystals can diffract to better than 2.8Å resolution. One completed dataset has been collected and it shows that the monomer orthorhombic Sau3AI/E64A crystal is in space group C2221 with unit cell parameters (69.44, 197.60, 191.46, 90, 90, 90) and contains two molecules in one asymmetric unit.

Keywords: crystallization; preliminary x-ray analysis; sau aI endonuclease

Document Type: Research Article


Publication date: May 1, 2007

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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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