title: Crystallization and preliminary X-ray analysis of a novel thermoalkalophilic poly(3-hydroxybutyrate) depolymerase (PhaZ7) from Paucimonas lemoignei.
abstract: Polyhydroxyalkanoates (PHA) are biodegradable polyesters that have attracted commercial and academic interest as environmentally friendly materials. A number of enzymes are able to degrade polyhydroxyalkanoates to water-soluble products. PhaZ7 poly(3-hydroxybutyrate) (PHB) depolymerase (EC 3.1.1.75), a 342-amino-acid hydrolase from the PHA-degrading bacterium Paucimonas lemoignei, has been found to possess substrate specificity for amorphous PHA. PhaZ7 was crystallized by the microdialysis method. Thin rod-like crystals were grown in low ionic strength solution and found to belong to the monoclinic space group C2, with unit-cell parameters a = 225.8, b = 46.5, c = 171.3, beta = 128.9 degrees. A complete data set was collected to 2.75 A resolution at 100 K using synchrotron radiation.
authors.affiliation: Turku Centre for Biotechnology, University of Turku, Tykistökatu 6, Turku 20521, Finland.
authors.forename: Evangelia G
authors.initials: EG
authors.lastname: Kapetaniou
authors.forename: Reinhard
authors.initials: R
authors.lastname: Braaz
authors.forename: Dieter
authors.initials: D
authors.lastname: Jendrossek
authors.forename: Anastassios C
authors.initials: AC
authors.lastname: Papageorgiou
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001673:Biodegradation, Environmental; D001704:Biopolymers / Q000737:chemistry; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006090:Gram-Negative Bacteria / Q000201:enzymology* / Q000378:metabolism; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D001704:Biopolymers; D002265:Carboxylic Ester Hydrolases; C438011:PHAZ7 protein, Paucimonas lemoignei