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Crystallization and Preliminary X-Ray Diffraction Analysis of ARO9, an Aromatic Aminotransferase from Saccharomyces cerevisiae

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Abstract:

Saccharomyces cerevisae ARO9 protein, an aromatic aminotransferase II, catalyzes the transamination step of the catabolism of aromatic amino acids, mainly tryptophan. ARO9 also belongs to a novel subfamily of enzymes within the aminotransferase subgroup I. Crystals of ARO9 protein have been grown using the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 75.6 Å, b = 117.5 Å, c = 134.9 Å. Diffraction data were collected to a resolution of 2.6 Å using a rotating-anode X-ray source. Analysis indicates the presence of two molecules in an asymmetric unit.





Keywords: ARO9; aminotransferase subgroup I; aromatic aminotransferase; crystallization; transamination

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986609787848036

Publication date: April 1, 2009

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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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