title: Crystallization and preliminary X-ray analysis of the trehalose/maltose ABC transporter MalFGK2 from Thermococcus litoralis.
abstract: Trehalose and maltose uptake in the hyperthermophilic archaeon Thermococcus litoralis is mediated by an ABC transport system. The heterotetrameric transport complex MalFGK(2), consisting of two membrane-spanning subunits and two copies of an ATP-binding cassette protein, has been crystallized. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 106.5, b = 150.5, c = 170.1 A, beta = 107.8 degrees. A native data set has been obtained at a resolution of 5 A.
authors.affiliation: Fachbereich Biologie, Universität Konstanz, M656, D-78457 Konstanz, Germany. andre.schiefner@uni-konstanz.de
authors.forename: A
authors.initials: A
authors.lastname: Schiefner
authors.forename: K
authors.initials: K
authors.lastname: Diederichs
authors.forename: K
authors.initials: K
authors.lastname: Hashimoto
authors.forename: W
authors.initials: W
authors.lastname: Boos
authors.forename: W
authors.initials: W
authors.lastname: Welte
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D019712:Thermococcus / Q000737:chemistry*
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins