Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa

Biological recycling of plant material is essential for biosphere maintenan ce. This perpetual task involves a complex array of enzymes, including extr acellular polysaccharide hydrolases and lyases. Whilst much is known about the structure and function of the hydrolases, relatively little is known ab out the structures and mechanisms of the corresponding lyases. To this end, crystals of the catalytic module of a novel family 10 pectate lyase, Pel10 A from Pseudomonas cellulosa, were obtained using polyethylene glycol 2000 monomethylether as a precipitant. They belong to space group P2(1), with un it-cell parameters a = 47.7, b = 106.1, c = 55.4 Angstrom, beta = 92.0 degr ees, and have two molecules in the asymmetric unit. The crystals diffract b eyond 1.5 Angstrom using synchrotron radiation.