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

Authors: Kusakabe Y.; Tanaka N.; Ito K.; Yoshimoto T.; Nakamura K.T.

Source: Protein and Peptide Letters, Volume 8, Number 3, June 2001 , pp. 237-240(4)

Publisher: Bentham Science Publishers

Buy & download fulltext article:

Price: $63.10 plus tax (Refund Policy)

Abstract:

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; Pseudomonas Putida; PFDH molecule; glutathione-dependent FDHs

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409454

Publication date: 2001-06-01

More about this publication?

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.