Crystallization and preliminary X-ray analysis of the bacterial ATP-binding-cassette (ABC) protein MalK
| Autor: | Günter Schmees, Erwin Schneider, Ulrich Ermler, K. Höner zu Bentrup, Daniela Vinzenz |
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| Rok vydání: | 1998 |
| Předmět: |
Salmonella typhimurium
ATP-binding cassette transporter Biology medicine.disease_cause Crystallography X-Ray law.invention chemistry.chemical_compound Bacterial Proteins Structural Biology law medicine Escherichia coli Molecule Crystallization Escherichia coli Proteins Resolution (electron density) General Medicine Maltose Recombinant Proteins Crystallography Membrane Biochemistry chemistry Cytoplasm ATP-Binding Cassette Transporters |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 55(Pt 1) |
| ISSN: | 0907-4449 |
| Popis: | 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)2SO4 as 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. |
| Databáze: | OpenAIRE |
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