Crystallization and preliminary X-ray analysis of the trehalose/maltose ABC transporter MalFGK2 from Thermococcus litoralis.
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.
Schiefner
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A
Fachbereich Biologie, Universität Konstanz, M656, D-78457 Konstanz, Germany. andre.schiefner@uni-konstanz.de
Diederichs
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K
Hashimoto
K
K
Boos
W
W
Welte
W
W
D019843:Archaeal Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D019712:Thermococcus / Q000737:chemistry*
D019843:Archaeal Proteins; D011994:Recombinant Proteins