title: Crystallization of barley (1-3,1-4)-beta-glucanase, isoenzyme II.
abstract: The (1-3,1-4)-beta-glucanase from barley (Hordeum vulgare, cv Alexis) degrades mixed linked beta-glucan in the cell wall of the starchy endosperm. Isoenzyme II of the (1-3,1-4)-beta-glucanase forms large single crystals when a protein solution is equilibrated against 20% (w/w) polyethylene glycol 8000 at acidic pH using the hanging drop vapour diffusion method. The crystals diffract to better than 2 A resolution. They are monoclinic, space group P2(1), with cell dimensions a = 49.58 A, b = 82.99 A, c = 77.56 A and beta = 104.36 degrees. Two protein molecules are estimated to fill the asymmetric unit.
authors.affiliation: Institut für Kristallographie, Freie Universität Berlin, Germany.
authors.forename: T
authors.initials: T
authors.lastname: Keitel
authors.forename: K K
authors.initials: KK
authors.lastname: Thomsen
authors.forename: U
authors.initials: U
authors.lastname: Heinemann
mesh_terms: D003460:Crystallization; D006026:Glycoside Hydrolases / Q000737:chemistry*; D001467:Hordeum / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D007527:Isoenzymes; D006026:Glycoside Hydrolases; C028020:licheninase