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Crystallizationand Preliminary X-Ray Crystallographic Studies of Formaldehyde Dehydrogenase from Pseudomonas putida

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The formaldehyde dehydrogenease from Pseudomonas putida (PFDH), has been crystallized by the vapour diffusion method using ammonium sulfate as the Precipitating agent. The crystals belong to a trigonal space group P3 12 (or P3 12) with the cell dimensions of a = b = 85.74 A, and c = 190.9 A. There are two subunits per asymmetric unit. The crystals diffract to at least 2.2 A resolution using Cu K Alfa radiation at 100 K. Self-rotation function studies suggest that the tetrameric PFDH molecular has the 222 point group symmetry.

Keywords: Formaldehyde Dehydrogenase; PFDH molecule; Pseudomonas Putida; glutathione-dependent FDHs

Document Type: Review Article


Publication date: June 1, 2001

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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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