title: Crystallization of halophilic malate dehydrogenase from Halobacterium marismortui.
abstract: Malate dehydrogenase from the extreme halophile Halobacterium marismortui crystallizes in highly concentrated phosphate solution in space group 12 with cell dimensions a = 113.8 A, b = 122.8 A, c = 126.7 A, beta = 98.1 degrees. The halophilic enzyme was found to be unstable at lower concentrations of phosphate. It associates with unusually large amounts of water and salt, and the combined particle volume shows a tight fit in the unit cell.
authors.affiliation: Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.
authors.forename: M
authors.initials: M
authors.lastname: Harel
authors.forename: M
authors.initials: M
authors.lastname: Shoham
authors.forename: F
authors.initials: F
authors.lastname: Frolow
authors.forename: H
authors.initials: H
authors.lastname: Eisenberg
authors.forename: M
authors.initials: M
authors.lastname: Mevarech
authors.forename: A
authors.initials: A
authors.lastname: Yonath
authors.forename: J L
authors.initials: JL
authors.lastname: Sussman
mesh_terms: D006217:Halobacterium / Q000201:enzymology*; D008291:Malate Dehydrogenase; D014961:X-Ray Diffraction
chemical_list: D008291:Malate Dehydrogenase