title: Crystallization and preliminary X-ray studies of the pectate lyase from Bacillus subtilis.
abstract: The pectate lyase (EC 4.2.2.9) from Bacillus subtilis has been crystallized. Crystals of form 1, grown by the hanging drop method using polyethylene glycol as precipitant, diffract to at least 2.4 A resolution. They belong to the spacegroup P2(1) with a = 132.9 A, b = 41.2 A, c = 156.8 A and beta = 114.9 degrees with probably four molecules in the asymmetric unit. A second crystal form grown from 2-methyl-2,4-pentandiol also belongs to the spacegroup P2(1) with a = 55.0 A, b = 88.1 A, c = 50.2 A and beta = 109.0 degrees. These crystals diffract to at least 2.0 A and have one molecule in the asymmetric unit. Both crystal forms are suitable for the determination of high-resolution structures.
authors: Department of Protein Engineering, AFRC Institute of Food Research, Reading, U.K.
authors: J
authors: J
authors: Jenkins
authors: W
authors: W
authors: Nasser
authors: M
authors: M
authors: Scott
authors: R
authors: R
authors: Pickersgill
authors: J C
authors: JC
authors: Vignon
authors: J
authors: J
authors: Robert-Baudouy
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D003460:Crystallization; D011092:Polyethylene Glycols; D011133:Polysaccharide-Lyases / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D011092:Polyethylene Glycols; D011133:Polysaccharide-Lyases; C023911:pectate lyase