title: Crystallization and preliminary crystallographic analysis of an amylopullulanase from the hyperthermophilic archaeon Pyrococcus woesei.
abstract: The thermostable amylopullulanase from Pyrococcus woesei was crystallized. Crystals, suitable for a crystallographic analysis up to a size of 0.6 mm in their longest dimension, have been obtained by the vapor diffusion method in a solution containing polyethyleneglycol 4000 (PEG 4000), isopropanol, and Tris/Cl- buffer pH 7.5. Crystals grown under these conditions form hexagonal rods and diffract to a maximum resolution of 3 A. The crystals belong to the trigonal lattice type with the spacegroup P3(1)21 or P3(2)21, respectively, have the cell dimensions a = b = 96.8 A, c = 196.2 A, alpha = beta = 90 degrees, gamma = 120 degrees. The crystals have a theoretical packing density of 2.7 A3/Da, assuming one molecule with a molecule weight of 88.8 kDa in the asymmetric unit. Furthermore the self-rotation analysis of the dataset revealed only crystallographic symmetries. The merged native data of two crystals resulted in a 88% complete dataset.
authors: Karolinska Institute, NOVUM, Huddinge, Sweden.
authors: S
authors: S
authors: Knapp
authors: A
authors: A
authors: Rüdiger
authors: G
authors: G
authors: Antranikian
authors: P L
authors: PL
authors: Jorgensen
authors: R
authors: R
authors: Ladenstein
mesh_terms: D001105:Archaea / Q000201:enzymology*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D016208:Databases, Factual; D004795:Enzyme Stability; D004926:Escherichia coli; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D006358:Hot Temperature; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; C100181:pullulanase