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Crystallization and preliminary X-ray analysis of the bacterial ATP-binding-cassette (ABC) protein MalK

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Vinzenz,  Daniela
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Schmees, G., Höner zu Bentrup, K., Schneider, E., Vinzenz, D., & Ermler, U. (1999). Crystallization and preliminary X-ray analysis of the bacterial ATP-binding-cassette (ABC) protein MalK. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 55(1), 285-286. doi:10.1107/S0907444998008518.


Cite as: http://hdl.handle.net/21.11116/0000-0007-A2E1-3
Abstract
The ATP-binding protein, MalK, of the bacterial ABC (ATP-binding-cassette) transport complex MalFGK2 provides the energy for the translocation of maltose and maltodextrins across the cytoplasmic membrane. The MalK protein from Salmonella typhimurium was overexpressed in Escherichia coli and crystallized by the hanging-drop method using (NH4)2SO4as a precipitant. The crystals belong to space group P6x22 (most probably x = 1 or 5) with cell dimensions a = 181.8 and c = 182.5 A, corresponding to three or four molecules per asymmetric unit. They diffract to a resolution of about 3 A on a synchrotron X-ray source and are suitable for structure determination.