title: Crystallization and preliminary X-ray crystallographic studies on 4-alpha-glucanotransferase from Thermotoga maritima.
abstract: Thermotoga maritima 4-alpha-glucanotransferase (GTase), a 52 kDa molecular-weight amylolytic enzyme, has been crystallized by the hanging-drop vapour-diffusion method using PEG monomethylether 5000 as a precipitating agent. A complete data set has been collected to 2.6 A resolution using cryocooling conditions and synchrotron radiation. The crystals belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 92.6, b = 180.3, c = 199.2 A.
authors: Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, England.
authors: A
authors: A
authors: Roujeinikova
authors: C
authors: C
authors: Raasch
authors: S
authors: S
authors: Sedelnikova
authors: W
authors: W
authors: Liebl
authors: D W
authors: DW
authors: Rice
mesh_terms: D018360:Crystallography, X-Ray; D006004:Glycogen Debranching Enzyme System / Q000737:chemistry*; D011487:Protein Conformation; D020124:Thermotoga maritima / Q000201:enzymology*
chemical_list: D006004:Glycogen Debranching Enzyme System; C020569:4 alpha-glucanotransferase