Crystallization and preliminary X-ray analysis of the trehalose/maltose ABC transporter MalFGK2 from Thermococcus litoralis

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Abstract

Trehalose and maltose uptake in the hyperthermophilic archaeon Thermococcus litoralis is mediated by an ABC transport system. The heterotetrameric transport complex MalFGK2, 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 Å, β = 107.8°. A native data set has been obtained at a resolution of 5 Å.

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Schiefner, A., Diederichs, K., Hashimoto, K., Boos, W., & Welte, W. (2002). Crystallization and preliminary X-ray analysis of the trehalose/maltose ABC transporter MalFGK2 from Thermococcus litoralis. Acta Crystallographica Section D: Biological Crystallography, 58(12), 2147–2149. https://doi.org/10.1107/S090744490201572X

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