title: Crystallization and preliminary crystallographic analysis of mannitol dehydrogenase (MtDH) from the common mushroom Agaricus bisporus.
abstract: Mannitol dehydrogenase (MtDH) is a key enzyme controlling the reductive synthesis of mannitol from fructose in the common mushroom Agaricus bisporus. A better understanding of the control of mannitol metabolism can be obtained by studying the structure of this enzyme. Here, the purification and crystallization of recombinant MtDH are reported. Crystals generally belonged to the space group C2, with unit-cell parameters a = 227, b = 125, c = 133 A, beta = 118 degrees, and diffracted to at least 1.8 A resolution, although a tantalum derivative belonged to the space group P2(1) and diffracted to the lower resolution of 2.9 A.
authors.affiliation: Department of Chemistry and Biochemistry, University of Berne, Freiestrasse 3, 3012 Berne, Switzerland. sassoon@izb.unibe.ch
authors.forename: J
authors.initials: J
authors.lastname: Sassoon
authors.forename: S
authors.initials: S
authors.lastname: Hörer
authors.forename: J
authors.initials: J
authors.lastname: Stoop
authors.forename: H
authors.initials: H
authors.lastname: Mooibroek
authors.forename: U
authors.initials: U
authors.lastname: Baumann
mesh_terms: D000363:Agaricales / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008354:Mannitol Dehydrogenases / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation
chemical_list: D008354:Mannitol Dehydrogenases